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chemistry that deals with the chemical compounds and processes occurring in organisms; and the chemical characteristics and reactions of a particular living organism or biological substance.
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biochem is the chemistry of what?
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biochem test 1
| Question | Answer |
|---|---|
| chemistry that deals with the chemical compounds and processes occurring in organisms; and the chemical characteristics and reactions of a particular living organism or biological substance. | biochemistry |
| biochem is the chemistry of what? | living matter |
| basic principles of biochemistry can be applied towards all living organisms. T or F | true |
| Glycolysis, an almost________ central pathway of glucose metabolism. | universal; greek - glykys = "sweet" and lysis = "splitting" |
| glycolysis - The chemistry of the glycolytic reaction sequence has been completely_________ in the course of evolution (common thermodynamic principles and the types of regulatory mechanisms). | conserved |
| biochemistry is _______ in our daily life | indispensible (absolutely necessary) - ex: eating lunch |
| what 4 things does biochemistry impact? | human biology and medicine, agriculture, industrial applications, and the environment (and more) |
| 5 important characteristics of living matter? | LECTURE 1 ANSWER |
| living matter - High degree of________ at molecular and organismal levels. | complexity |
| living matter must be able to Extract, transform, and utilize______ from their environment for maintenance, regeneration, and function. | energy |
| energy _______ and _______ keep organisms alive | transduction; transformation |
| living systems extract energy from what two main sources? | 1) from sunlight - plants, green bacteria, cyanobacteria 2) from nutrients/fuels- animals and most bactiera |
| living matter must be able to ________ between self and non self and ______ and _______ to change in the surrounding; immune system recognizes a bacteria, virus, etc. and mounts an immune response | distinguish; sense; respond |
| living matter - regulated interactions between individual components that are ______ and ________ ex: cell signaling map and brain signaling for movment | dynamic; coordinated |
| living matter - fairly _______ self replication (DNA) while allowing enough _____ for evolution. biological reproduction with near-perfect fidelity | precise; change |
| 3 distinct domains of life? prokaryotes or eukaryotes? | prokaryotes: bacteria and archaea eukaryotes: eukarya |
| structural heirarchy of living matter? | elements --> monomers --> polymers --> supramolecular structures --> organelles --> cells --> tissues --> organisms |
| simple organic compounds | monomers |
| macromolecules | polymers |
| most abundant essential elements (structural components) | C, H, O, N, P, S |
| less abundant essential elements (homeostasis) | Na+, K+, Ca2+, Cl- |
| trace amounts of these essential elements (metabolism, enzymatic cofactors) | Mg++, Zn++, Fe++, Mn++, Cu++ |
| what simple organic compound? components: nitrogenous base, five carbon sugars, phosphate | nucleic acids |
| what simple organic compound? long chains of hydrophobic, insoluble | lipids |
| what simple organic compound? parent sugar is glucose | carbohydrates |
| macromolecules - biological molecules typically have multiple _______ _______ | functional groups |
| GO OVER COMMON FUNCTIONAL GROUP FLASH CARDS HOE | |
| interactions between biomolecules are _______ | specific. |
| 1. Macromolecules have______ binding domains. 2. Only certain molecules can bind – ______ and ______. 3. Binding of chiral biomolecules is________. | specific; lock and key; stereospecific |
| Biological Molecules’ Function Depends on ______ ______ Structure | Three-Dimensional |
| biological molecules function depends on 3D structure - what were the 4 3D structures we talked about? | 1) geometric isomers (cis vs trans) 2) stereoisomers (four, 2 asymmetric carbon) 3) enantiomers (mirror images, 2 pairs) 4) diastereomers (all non-mirror image pairs) |
| major macromolecules? (4) | proteins, nucleic acids, polysaccharides, lipids |
| what is structural hierarchy: molecules --> cells? | monomeric units (nucleotides, amino acids, sugars) --> marcomolecules (DNA, protein, cellulose) --> supramolecular complexes (chromatin, plasma membrane, cell wall) --> cell/organelles |
| • All living organisms are made of______. • Cells are NOT all the same. • The simplest living organisms are_______-celled. • Larger organisms consist of many cells that are different in _____, _____, and _______ | cells;single; origin, morphology, and function. |
| what do eukaryotes have that prokaryotes don't? | eukaryotes have nucleus, nuclear membrane, and membrane bound organelles and because of compartmentalization, they have spatial separation of energy yielding and energy consuming reactions |
| PROKARYOTE VS EUKARYOTE LECTURE 1 | |
| life is a coordinted series of _______ reactions | chemical |
| 2 parts of metabolism? | catabolism and anabolism |
| part of metabolism that is oxidative, destructive, and releases energy ; goes from a complex thing (stored nutrients) to a small molecule; energy released as ATP or NADPH | catabolism |
| part of metabolism that is reductive, constructive, and stores energy; goes from simple molecules to complex molecule; low energy --> high energy molecules and requires in put of ATP and reduced electron carrire | anabolism |
| catabolic reaction pathways are _______ and anabolic reaction pathways are __________ | exergonic; endergonic |
| anabolic pathways proceed ________ with catabolic pathways in a dynamic steady state | simultaneously |
| example of catabolism? | oxidation of glucose (C6H12O6 + 6O2 --> 6CO2 AND 6H20 |
| catabolism is oxidative and degradative; it generates _______ and reduces ________ | ATP; coenzymes ; lecture 2 page 1 catabolism |
| release of energy | exergonic |
| why is ATP the chemical currency of energy? | phosphoanhydride bonds are high energy --> broken, energy released |
| . For any physical or chemical change, the total amount of energy in the universe remains constant; 2. Energy may change form or it may be transported from one region to another, but it can not be created or destroyed. | thermodynamics - principle of the conservation of energy |
| Cells are efficient_______ of energy (convert energy from one form to another) , capable of interconverting _____, ________, _______, and _______ energy with great efficiency. | transducers; chemical, electromagnetic, mechanical, and osmotic |
| ; Living cannot create energy; Living cannot destroy energy (“used up”).; Living organism may_______ energy from one form to another (e.g., energy stored in chemical bonds into kinetic energy of heat and motion). | ; convert |
| organisms perform energy ______ to accomplish work and stay alive | transduction - lecture 2 |
| Anabolic pathways________ cellular components from simple precursor molecules; _______ chemical energy (ATP and NADH or NADPH); they are ______ when compared to oxidative catabolic pathways | synthesize; Consume; reductive |
| “New formation of sugar” that converts pyruvate and related three- and four-carbon compounds to glucose. | gluconeogenesis |
| in gluconeogenesis, Essentially same reactions in all tissues and all species. The_______ context and the________ of gluconeogenesis differ between species and tissues. | metabolic; regulation |
| important gluconeogenesis precursors in animals? | lactate --> pyruvate, glucogenic amino acids, and glycerol |
| process that requires energy | endergonic |
| The universe always tends towards increasing disorder: in all natural processes, the entropy of the universe increases. | second law of thermodynamics |
| (the amount of energy capable of doing work during a reaction at constant temperature and pressure). | gibbs free energy |
| the heat content of the reaction system). | enthalpy (H) |
| a quantitative expression for the randomness or disorder in a system). | entropy (S) |
| a ______∆G is a favorable reaction - ___∆S and ____∆H | negative (exergonic) +∆S - increasing disorder; products more disordered than reaactants -∆H - release heat |
| relationship between ∆G, ∆H, and ∆S in biological systems for constant temp and pressure | ∆G = ∆H - T∆S |
| _______ΔG: endergonic reaction that gains free energy. _______ ΔG: exergonic reaction that releases energy. | Positive; Negative |
| ü Endergonic ü ΔG > 0 ü Reactants are stable ü Reaction is not spontaneous | unfavorable - ex: synthesis |
| ü Exergonic ü ΔG < 0 ü Products are stable ü Reaction is spontaneous | favorable - ex: breakdown |
| Chemical________ of exergonic and endergonic reactions allows otherwise unfavorable reactions. • The “high-energy” molecule (______) reacts directly with the metabolite that needs “activation.” | coupling; ATP ∆G3 = ∆G1 + ∆G2 |
| A thermodynamically unfavorable (endergonic) reaction can be driven in the forward direction by coupling it to a thermodynamically favorable (exergonic) reaction through a_______ ________ | common intermediate; LECTURE 2 EQUATION!! |
| kinetics - intermediate between substrate and product;unstable; and distinct conformation. | transition state - lecture 2 page 5 |
| kinetics - energy required to reach the transition state. | activation energy |
| the higher the activation energy, the _______ the reaction rate | slower |
| At the equilibrium concentrations of substrates and products, the forward rate_____ the reverse rate and there is no further______ in the system. | equals; change |
| When a reaction is not at equilibrium, the driving force that moves the reaction towards equilibrium is expressed quantitatively as the free energy change for the reaction, _____. | ΔG |
| Keq =? | EQUATION ON LECTURE 2 PAGE 5 |
| For chemical reactions, ΔG'o is dependent on the ______ | K'eq. - KNOW THIS EQUATION LECTURE 2 PAGE 6 |
| with a larger Keq, that means the concentrations of products are increased, and standard free energy change (∆G) is more negative, which means its more ________ | favorable ; large Keq = favorable ∆G |
| when Keq is greater than 1, ∆G is negative, and starting with all components at 1M, the reaction proceeds _______ | forward |
| when Keq = 1, ∆G is zero, and starting with all components at 1 M the reaction is ___________ | at equlibirum |
| when Keq <1, ∆G is positive and starting with all components at 1 M then the reaction proceeds _________ | in reverse |
| v Standard free energy change (ΔG'o): • Standard conditions- initial concentration of each component is 1.0 M, 25°C, pH 7, and 101.3 kPa. • Characteristic and unchanging________ for a given reaction. | constant |
| Living cells are different from test tubes!_______ free energy change (ΔG) (not standard) determines the spontaneity of a reaction. ∆G (actual) = ∆G (standard) + RT lnKeq | Actual |
| how to speed up reactions, that would work in test tube but not suitable for living organisms | -Higher temperatures (may destabilize macromolecules) -Higher concentrations of reactants (need more valuable starting material) |
| how to speed up reactions, that would work in living organisms? | -Lower activation barrier by catalysis (i.e., enzymes) - Change the reaction by coupling to a fast one |
| Enzymes Lower the _____ ______ to Increase the Reaction Rate | Activation Energy |
| LECTURE 2 NOTES - CHANGE REACTION BY COUPLING WITH A FAST ONE NOTES ! | |
| who did this experiment? Abiotic formation of organic compounds under primitive atmospheric conditions; “Primordial Soup” Simple Organic Compounds (Biomolecules) | miller and urey |
| evolutionary benchmarks - Modern Humans ________y ears ago First land vertebrates _______ years ago | 160,000 ; 350,000,000 |
| Life evolved in______. Biochemical reactions often occur in______ setting. ______ is Crucial for the structure and function of biomolecules and most abundant substance in living organisms - why it is so important for life | water; aqueous; water |
| water is a good solvent for _____ and _____ substances (amino acids, peptides, carbohydrates - hydroxyls, nucleic acids, etc) | charged; polar |
| water is a poor solvent for ________ substances (nonpolar gases, N2, O2, lipids, others) | NONPOLAR |
| required for degradation for high energy chemicals (oxidation), so because our blood is aqueous, water is poor solvent for oxygen so need proteins to carr it | oxygen |
| molecule that has both polar and nonpolar grups | amphipathic |
| what has a higher solubility in water? oxygen or CO2? why? | CO2 - oxygen has poor solubility in water. O2 is very nonpolar, and so is CO2 but CO2 has some partial negative on the oxygens |
| ________of the oxygen atom induces a net dipole moment (2 electric dipoles per water molecule, one along each of the H−O bonds). | Electronegativity |
| water molecule's shape is a distorted _______ | tetrahedron - 2 pairs bond to H and 2 lone pairs |
| Each water is able to form H-bonds with as many as___ other water molecules. • H-bond distance is____ times the distance between the covalent O and H bond. energy to break H-bond vs energy to break the covalent O-H bond: __: __ | 4; 2; energy to break H-bond vs energy to break the covalent O-H bond: 1:20 |
| In ice, each water molecule can form hydrogen bonds with four neighboring water molecules. A crystal lattice structure makes ice less_____ than liquid water, and thus ice floats on liquid water. | dense |
| Melting of ice and evaporation of water occur_______ at room temperature. ΔG = ΔH − TΔS; melting and evaporation at room temp have +∆H --> release heat and ∆S - increase entropy | spontaneously - ∆G is negative |
| 4 noncovalent bonds? | hydrogen, ionic, van der waals, hydrophobic |
| for hydrogen bonding you have to have an _______, and a _________. water can serve as both of these | acceptors and donors; hydrogen acceptors differ as long as its partial negative/ has LP, but donor has to have a hydrogen that has a partial positive |
| a hydrogen bond in a biomolecule is stronger when it is ________ rather than when it is ________ | direction and strength; straight - stronger, bent - weaker |
| ionic interactions are Electrostatic interactions between permanently_______ species • Electrostatic interactions between the_____ and a permanent______ | charged; ion; dipole |
| ion-dipole interactions - Water is dipole that interacts electrostatically with charged solutes by orienting H toward______ and O toward______. | anions; cations; water and NaCl |
| Van der Waals interactions are: • Weak interatomic attractions (reversible, easily broken) • Universal: occur between two _______ atoms that come next to each other | uncharged |
| which noncovalent forces are important to determine steric complementarity • stabilize biological macromolecules (stacking in DNA) • facilitate the binding of polarizable ligands | van der waals |
| 2 components of van der waals? | attractive and repulsive force |
| van der waals force that (London dispersion) that dominates at longer distances (typically 0.4-0.7 nm). | attractive |
| van der waals (Steric repulsion) that dominates at short distance. | repulsive |
| compounds that have hydrophilic group and hydrophobic group | amphipathic |
| hydrophobic interactions - lipid in water, water will try to form cage and they are highly ordered --> entropy decreased. so the lipid ______ and hydrophobic groups condense and releases trapped water and allows entropy to increase bc random h20 released | aggregates |
| • amphipathic • nonpolar group in the middle • polar group facing out, interacting with water • energy wise – more favorable ; minimize ordered shell of water molecules; increase entropy of water | micelles |
| _____Interactions are Crucial to Macromolecular Structure and Function | Weak - summary lecture 3 |
| Certain properties of solution such as boiling point, melting point, and osmolarity that do not depend strongly on the chemical nature of the dissolved substance. | colligative properties |
| Properties such as viscosity, surface tension, taste, and color, etc. that depend strongly on the chemical nature of the solute. | non-colligative properties |
| Cytoplasm of cells are highly_______ solutions and have high_______ pressure. | concentrated; osmotic |
| the measure of solute concentration | osmolarity |
| _______ - No net movement of water. ü _______solution- Water moves out and cell shrinks. ü ______solution - Water moves in and cell burst. | Isotonic; Hypertonic; Hypotonic |
| it is very rare that 2 water molecules connected by a hydrogen bond disassociate into hydronium ion (H3O+) and hydroxyl ion; most water remains _______ in the pure water form | uncharged |
| what is wrong with this commonly seen formula? H2O --> H+ + OH- | free protons do not exist in solution; proton H+ is written in place of H3O+ |
| ionization of water - ______ ______:rapid net movement of a proton, because the covalent and H- bonds are interchangeable. very rapid | proton hopping ; lecture 5 page 1 |
| proton hopping applies to the hydroxyl ion in water, except in the ________ direction | opposite |
| constant that is a Fixed value that is characteristic for each specific reaction. concentration of products over reactants ; determined by electrical conductivity measurements | equilibrium constants - Keq |
| equilibrium constant for water? | 1.8 x 10^-16 M |
| Kw, ion product of water is equal to what? | Keq x [H2O] or [H+]x[OH-] |
| at pH=7, the concentration of[H+] and [OH] are what? Kw = [H+][OH-]= 1 x 10^-14 M^2 | equal to each other... so [H+]=[OH-] soooo [H+][OH-] = [H+]^2 SOOOO SQUARE ROOT OF THAT GIVES 1 X 10^-7 =[H+] |
| a mathematical term that means the negative log of. | p |
| pH = what mathematically? | -log [H+] |
| pH + pOH = ? | 14 |
| alkaline conditions [H+] lower [OH-] higher... pH is what? | pH > 7 |
| neutral condition water, [H+] = [OH-] | pH = 7 |
| acidic conditions [H+] greater; [OH-] smaller | pH <7 |
| GO OVER LOGS AGAIN | |
| strong acids and bases completely dissociate in water and there is no equlibrium T or F | true |
| Strong Acid + Strong Base = ??? HCl + NaOH | Water + Salt |
| acids that only dissociate to a limited degree in water | weak acids |
| for weak acids, the extent of dissociation is ___-dependent | pH |
| for weak acids: ow pH, high [H+] push the reaction to the______ very little of the weak acid will be dissociated into ions. | left; HA (equilibrium arrows) (H+) + (A-) increase H+, shift towards the left |
| for weak acids, high pH, low [H+] push the reaction to the_____ most of the weak acid will be dissociated into ions. | right; HA (equilibrium arrows) (H+) + (A-) |
| acid dissociation constant | Ka = [H+][A-]/[HA] |
| LOOK AT HENDERSON-HASSELBACH | |
| weak acids - When the pH = pKa, ____ _____ of the weak acid will be dissociated into ions. | one half |
| when [A-] =[HA], then pH=? | pH = pKa; pH = pKa + log([A-]/[HA]) = pKa + 0 = pKa |
| LECTURE 5 PAGE 6 TITRATION | |
| when pKa = pH, the weak acid is ______ dissasociated | 50% |
| based on pKa values out of these 3 weak acids, which is strongest and which is weakest? titration curve: [CH3COOH] = [CH3COO-] pH = pKa = 4.76 [H2PO4–] = [HPO42–] pH = pKa = 6.86 [NH4+] = [NH3] pH = pKa = 9.25 | Acetic acid is the strongest acid (pKa = 4.76). - lowest pKa Dihydrogen phosphate is in the middle (pKa = 6.86). Ammonium ion is the weakest acid (pKa = 9.25). |
| the smaller the pKa, the ________ the acidity | stronger |
| what is the conjugate acid base pair? which is proton donor which is proton acceptor? CH3COOH (equilibrium arrows) H+ + CH3COO- | acetic acid and acetate are conjugate acid/base pair; acetic acid is proton donor and acetate is proton acceptor |
| acid that gives up only one proton - CH3COOH(equilibrium arrows) H+ + CH3COO- | monoprotic |
| acid that gives up two protons;H2CO3 --> H+ + HCO3- pKa = 3.77 HCO3- --> H+ + CO32- pKa = 10.2 | diprotic acid |
| acid that gives up three protons (H3PO4) | phosphoric acid |
| for diprotic and triprotic, which is the stronger weaker acid? | the first proton removal is always the strongest weak acid |
| Almost every biological process is_____- dependent. A small change in pH produces a______ change in the rate of the process. | pH; large |
| Cells and organisms maintain a specific and constant______ pH (usually pH 7.0) to keep biomolecules in their optimal ionic states. Biological______ – mixtures of weak acids and their conjugate bases are employed to achieve pH________. | cytosolic; buffers; constancy |
| aqueous systems that resist changes in pH when small amounts of acid (H+) or base (OH-) are added. | buffers |
| Buffer is composed of a______ acid (proton donor) and its ______ _____(proton acceptor). Each conjugate acid-base pair has a characteristic pH zone to function as an effective buffer. | weak; conjugate base |
| a flat zone on the titration curve – addition of given amounts of acid (H+) or base (OH-) has less effect on pH that outside the zone. EX: acetic acid, pH=pKa @4.76, this region is between 3.76 and 5.76 for acetic acid/acetate | buffering region |
| 2 important physiological buffers? | phosphate and bicarbonate |
| important physiological buffer that acts in cytoplasm of cells - In mammals, extracellular fluids and most cytoplasmic compartments have a pH in the range of 6.9 to 7.4. | phosphate buffer system - pH 5.9 to 7.9 H2PO4 --> H+ + HPO4 - |
| which important physiological buffer? good for blood plasma buffer; effective buffer near pH 7.4, the pH depends on concentrations of CO2 gas, dissolved CO2 converted into H2CO3 and HCO3- | bicarbonate buffer; H2CO3 --> H+ + HCO3- carbonic acid (H2CO3) is from dissovled CO2 and water |
| when the CO2 bicarbonate buffer system is disrupted, pH<7.35 and you get what condition? | acidosis - pathological condition or exercise |
| the most abundant biological macromolecules, found in all cells and all parts of cells. | proteins |
| Proteins are the main agents of biological functions, mediating virtually every process in a cell. • Proteins are_______ in both structure and function. | diverse |
| building blocks of proteins | amino acids |
| Proteins (from bacteria to human beings) are constructed from a common set of____ amino acids. | 20; |
| Cells produce structurally and functionally diverse proteins by covalently linking the same 20 amino acids in different ________ and ________ | combinations and sequences. |
| general structure of alpha amino acids - a carboxyl group and an amino group bond to the same alpha carbon - applies to 19 of the AAs but not ________ why? | proline is cyclic |
| 2 conventions to identify carbons: | organic nomenclature and biochemical designation |
| identifying carbons in proteins 12 conventions: _______nomenclature: start from the carboxyl end. • _______ designation: start from the α-carbon and go down the R-group. | Organic; Biochemical |
| the alpha carbon is ________ in 19 common amino acids, but not glycerine; which means there are two possible stereosiomers that are nonsuperimposable mirror images or what? | chiral ; enantiomers |
| for most amino acids, if the amino group is on the left and R group below, it is "___" conformation but if amino group is on the right and R group below it is "____" conformation | L, D |
| L and D only refer to the absolute configuration of the four substituents around the chiral α-carbon in amino acids. Virtually all amino acid residues in proteins are____ stereoisomers. | L |
| Cells use enzymes with_________ active sites to select L amino acids! | asymmetric |
| Depending on the R substituents, the 20 common amino acids can be placed into______ groups. R groups vary in structure, size, charge, and solubility in water | five |
| AMINO ACID FLASHCARDS! | |
| Amino acids that are Not incorporated by ribosomes.Post-translational modifications of proteins. • Important biological functions. For example, reversible phosphorylation that is important in signaling. | uncommon amino acids |
| lecture 6 biochem page 6 post translational modification | |
| in a reducing agent, a disulfide bond would be _______ in cystine to form 2 cysteine amino acids with sulflhydryl bonds | broken |
| ionization of amino acids - At acidic pH, the______ group is protonated and the amino acid is in the cationic form. | carboxyl |
| ionization of amino acids - At neutral pH, the carboxyl group is______ but the amino group is______. The net charge is zero; such ions are called______. | deprotonated; protonated; Zwitterions |
| ionization of amino acids At alkaline pH, the amino group is______ : NH2 and the amino acid is in the anionic form. | neutral |
| amino acid net charge is zero | zwitterions - lectrue 6 page 6 |
| titration of amino acid notes and lecture lecture 6 page 7 notes and highlighted notes | |
| α-carboxyl group is much_____ acidic than in carboxylic acids • α-amino group is slightly_____ basic than in amines | more; less -- because of unique structure of amino acid it is not pure acid or pure base pKa of acetic acid = 4.8 but for carboxyl group is 2.34 pKa of methylamine is 10.6 and for alpha amino acid is 9.6 |
| Zwitterions_______ at pH values between the pKa values of the amino and carboxyl groups. | predominate |
| For amino acids without ionizable side chains, the Isoelectric Point (equivalence point, pI) is = ??? | pI = Pk1 + pK2/ 2 the average of pK's |
| At the isoelectric point, AA: o net charge is_____ o ______ soluble in water o does not_____ in electric field | zero; least; migrate |
| Ionizable side chains can be________. • Titration curves are more complex. • pKa values are discernable if two pKa values are more than two pH units apart. | titrated |
| how do you calculate pI with more than 2 ionizable things in side chains? | 1) identify zwitterion (net charge = 0) 2) identify pKa that defines ACID strength 3) identify pKa value that defines base strength 4) average those 2 pKa values - lecture 6 page 8 |
| at pH = 7 Aspartate and Glutamate are______ charged • Lysine and Arginine are________ charged • ________ may be positively charged or uncharged | negatively; positively; Histidine MAKE SURE LECTURE 6 PAGE 8 MEMORIZE CHART IS IN THERE |
| biochem lecture 6 notebook notes | |
| Peptides are chains of amino acids covalently joined through a substituted amide linkage, termed a _____ ______ | peptide bond. |
| peptide bonds are formed from a __________ reaction | condensation - loses water; OH on COOH and H oh NH2 |
| the peptide bond: is less_______ (more stable) ² exhibits_______ moment in the trans configuration (favored) ² is______ and nearly________ (this one has to do with structure) | reactive; dipole; rigid; planar |
| The peptide bond has some________ bond character, because of the resonance or partial pairing between the carbonyl oxygen and the amide nitrogen. | double; chem 471 09_06 lecture page 1 |
| in a peptide, which bonds can rotate? | the alpha carbon-C bond can rotate and the alpha carbon and nitrogen can torate, but the carbon nitrogen bond is RIGID and cannot rotate |
| in peptides, numbering starts from the _______ terminal (left) to the _______ terminal (right) | N-terminal to C-terminal |
| CHAPTER 3 PROBLEM 11 | answer in notes biochem lecture 6 and on laptop highlight |
| No generalization can be made to relate the size of peptides and proteins to their functions. True or False? | true ; Naturally occurring peptides range from 2 amino acid residues to many thousands. bioactive small peptides - hormones, pheromones, neuropeptides, toxins |
| terminology for few amino acids in a peptide | oligopeptides |
| terminology for many amino acids in a peptide | polypeptide |
| generally, polypeptides have a molecular weight less than ???? and proteins have a molecular weight greater than ???? the average weight of an amino acid is ???? | 10,000; GENERALLY - EACH AMINO ACID THE AVERAGE WEIGHT IS 110 G |
| proteins are made of polypeptides, but polypeptides are NOT made of protein. T or F | true |
| proteins may contain: a single polypeptide; two or more polypeptides held by both _______ and _________ interactions | noncovalent; covalent |
| • Proteins may contain: – _______ (metal ions or organic molecules). – ________ (organic compounds, e.g. NAD+) – ________ groups (covalently attached cofactors, e.g. heme) – Other modifications. | Cofactors; Coenzymes; Prosthetic |
| proteins that contain permanently associated chemical groups, in addition to amino acids. | conjugated proteins |
| ________group is the non-amino acid part of a conjugated protein. | Prosthetic; 09/06 lecture page 5 table 3-4 |
| Protein function depends on its _____ _______sequence. classical methods sequence one amino acid at a time | amino acid sequence = identity). |
| The amino acid sequences of millions of proteins have been determined indirectly by_______ sequencing. • Automation and_______ spectrometry provide faster alternative methods to determine amino acid sequences. | DNA; mass |
| before sequencing a protein, what must be done first? | purify the target protein and reducing the level of complexity by cleaving it into smaller peptides by proteases or chemicals and then sequence each peptide |
| in protein methods, for proteolysis, Some proteases cleave proteins into smaller polypeptides, by catalyzing the hydrolytic cleavage of the peptide bond adjacent to particular _____ _______residues. | amino acid |
| for protein methods, in order to break up proteins into smaller pepties to sequence, how do you break a disulfide bond in say insulin? | oxidizing and reducing agents |
| what protein method? Identify one amino acid residue from the N-terminal at a time; repeat; sequence up to 40 sequential residues. attach chemical group to N-termianl end, cleave, then identify AA one at a time | chemical sequencing - edman degradation |
| what molecules are to be analyzed in mass spectroscopy? | analytes |
| analytes are ü ionized in a vacuum ü introduced into an electric or magnetic field ü measures mass to charge ratio (m/z) | mass spectroscopy |
| how does mass spectroscopy sequence proteins/peptides? | each AA has a specific mass to charge ratio (m/z) and then you assemble the peptide sequence based on m/z values |
| when membrane has this lipid, it allows the membrane to curve which allows machinery for ETC in mitochondria; required for mitochondrial structure and function | cardiolipin |
| when laying out a research plan, you want to monitor the _________ for all throughout the isolation process. (ex: change pH --> protein can change conformation) | bioactivity |
| in research plan: lyse cells /cell structure breaks apart = __________ separate organelles from cell debris/ separate soluble proteins from insoluble proteins = __________ | homogenation; centrifugation |
| in research example with CLS, to separate CLS protein from other components is done by _________, analyzing the CLS protein is done by _______, and resolving the structure of the CLS protein is done by ________ | chromatography; electrophoresis; sequencing |
| protein methods: Two components (to be performed repeatedly): o Determine the protein concentration for monitoring yield. o Assay for CLS activity do this for each step during separation proceudre | bioassay-guided isolation - "quality control" that just makes sure sample is active before initiating isolation effort |
| separates substances based on density | centrifugation |
| on low speed for centrifugation of homogenized tissue, there are what 2 main densities/ | supernatant - organelles and pellet that contains whole cells, nuclei, cytoskeleton,e tc. |
| on high speed for centrifugation of homogenized tissue, there are what 2 main densities/ | supernatant - smaller subcellular structures pellet - mitochondria, lysosomes, peroxisomes |
| how do you use centrifugation to separate organelles? aka separate mitochondria, lysosomes, peroxisomes etc after regular centrifugation? | sucrose density centfigugation -- prepare series of sucrose solutions and different layers of sucrose with different densities then poke hole and collect fraction |
| how do you acquire soluble proteins in protein methods? lecture 09/08 page 3 | centrifugation to separate soluble proteins from isnoluble; place them in a hypotonic solution and water gushes in cell and lyses it; only thing left is insoluble proteins and membrane components, and soluble proteins in solution |
| chromotagraphy is used in protein _________ | separation |
| 3 phases of chromotagraphy | stationary, mobile, effluent |
| solid porous matrix inside the column. what chromotagraphy phase? | stationary |
| the solution pumped into the column. what chromotagraphy phase? | mobile |
| the solution that comes out of the column, collected as fractions. what chromatagraphy phase? | effluent |
| Three Chromatographical Methods for Protein Purification: | ion exchange, size exclusion, affinity |
| 2 types of ion exchange chromatography | anion exchange and cation exchange |
| ion exchange chromatography - AnionExchange 1. Matrix (____) charged. 2. Proteins (____) bind. 3. Elution: High salt,________ conditions. | + (positively) ; negative; acidic - bc column is positive, protein are negative, want to pull protein from positive matrix, the acidic solution gives more protons and helps protein fall off the matrix |
| cation ion exchange chromatagraphy - Matrix (_____) charged. 2. Proteins (______) bind. 3. Elution: High salt,_________ conditions. | negative; positive; basic - negatively charged basic eludes and pulls positive proteins from negative matrix |
| with cation ion exchanges in chromatography, proteins with a more ________ charge will move faster and elute earlier | negative |
| ch 3 problem 17 | in notebook biochem lecture 7 |
| in size exclusion chromatography, 1. Larger molecules elute_______ . 2. Smaller molecules elute _______. | first; last ; smaller can get stuck in matrix and larger cannot |
| chromatography where separation by binding specificties between ligand and a protein | affinity chromatography |
| how does affinity chromatography work? | immobilized ligand is linked to the matrix. protein of interest binds to the ligand. unwanted proteins washed through the column protein of interest is eluted with ligand solution |
| with affinity chromatography, how do you remove ligand from protein of interest once it is out of the column? | dialysis |
| in electrophoresis, Gel matrix_______ the mobility of proteins according to their size and shape. and Running buffer_________ electricity. | hinders; conducts |
| in electrophoresis, what electrode to they migrate to? | from negative to positive |
| After electrophoresis: the proteins can be visualized by staining the gel (i.e., Coomassie blue).Each band corresponds to a ________. small migrate faster compared to larger proteins | protein |
| what does SDS page do to a protein? | proteins can have different charges, so it is a negative detergent that makes all proteins negative so it eliminates charge. it also eliminates shapes of proteins by denaturing it into a long strand. so all that it does is spearate by WEIGHT |
| how do you find relative migration? on a gel | distance traveled on gel/total gel length |
| PROTEIN METHODS - ESTIMATE MW BY SDS PAGE LOOK AT lecture 09/08 | |
| what are the 2 dimensions in 2D electrophoresis? | first - isolectric focusing on pI point and charge second: SDS-PAGE - molecular/weight and size |
| 2D electrophoresis resolves hundreds of distinct proteins and provdies a snapshot of relative protein abundance ; adds in another dimension to separate proteins apart | ok |
| Isoelectric focusing (2D electrophoresis) Separate native proteins according to their______ _________ 2. Ampholytes establish a stable pH gradient on a gel strip. 3. In an electric field, proteins migrate to pH = pI (protein net charge is____). | isoelectric points.; zero |
| Protein molecules adopt a specific 3-dimensional conformation (called the _____ _______). this conformation is mainly held together by favorable_________ interactions. | native fold; noncovalent |
| Proper folding of a protein requires________, because of the decrease in conformational entropy. | energy |
| protein structure: AA sequence that determines function | primary |
| protein structure: Local folding: α-helix, β-sheet, random coil | secondary |
| protein structure: “Global” folding of a single polypeptide chain | tertiary |
| proteins tructure: Subunit arrangement: assembly of folded proteins into multi-subunit macromolecules– dimer, trimer, tetramer, etc. | quaternary |
| if a protein is a single polypeptide, can it form a quaternary structure? | no - bc it doesn't have multiple subunits |
| peptide bond________ links amino acids in a protein molecule. | covalently |
| Secondary structure: a local three-dimensional folding of the polypeptide chain. • Defined by patterns of________ bonds between the backbone amide groups. and between 2 different peptide BONDS, not same peptide bond | hydrogen |
| secondary protein structure: Chain is coiled like a spring, Held together by H- bonds between nearby residues; R groups protrude outwards ; very compact, peptide bonds align roughly parallel with helical axis | alpha helix |
| alpha helix is a Very________ structure: • Inner diameter: 4 – 5 Å, too small for anything to fit ‘inside’ • Outer diameter (with side chains): 10 – 12 Å, fits into dsDNA major grove | compact |
| Peptide bond has a strong dipole moment. "Carbonyl O negative "Amide N positive • The___ _____ secondary protein structure has a large macroscopic dipole moment. carboxylic end is negative and amino terminus is positive | α helix ; dipole between N+ and O-... |
| _________Affects α-Helix Stability | Sequence |
| Strong alpha helix formers: ______, ___________ amino acid residues (e.g., Ala and Leu) | small hydrophobic |
| alpha Helix breakers: _____ (cyclic R-group, can’t rotate). _____ (tiny R-group (H) supports other conformations) | Pro; Gly |
| why can't proline rotate well? | because between peptide and R group, the R can usually rotate, but proline can't because it is cyclic and attached to the amino group |
| beta strand: Extended peptide chains naturally make a pleated geometry. • α-Carbons are the_______. • R-groups________ (up, down, up, down....) • Planar peptide bonds are in the_______. | apices; alternate; pleat |
| what secondary structure for protein? -Peptide chains align side-by-side. -Interstrand H-bond-Parallel and Antiparallel | beta SHEET |
| same direction of beta sheet vs opposite direction beta sheet | parallel and antiparallel |
| Connecting elements that link segments of α helix and/or β sheet. | beta turn |
| _______ or _______ residues are commonly found in beta turns | Proline or glycine |
| type I beta turn: | • Proline in 2nd position. • Proline: conformationally restricted with fixed φ angle, keeps turn rigid. |
| type 2 beta turn: | Glycine in 3rd position • Glycine: small and flexible, allows for tight corners. |
| type 1 beta turns occurs _____ times more frequently than type 2 | 2 |
| for type 1 and 2 beta turns, why can't glycine or proline be in 1 or 2 AA position? | becaust there is a H-bond between carbonyl oxygen in AA1 and amino group hydrogen in AA 2 |
| Peptide bond configuration: • Nearly all peptide bonds not involving proline are in the_______ configuration (>99.95%). | trans |
| Peptide conformation is defined by dihedral angles (or torsion angles). Dihedral angles: o Φ (phi): what angle? ψ (psi): ? | phi - angle between nitrogen and alpha carbon psi - angle between alpha carbon and carbon |
| with ramachandran plot, it shows the distribution of phi and psi dihedral angles that are found in a protein. certain secondary structures can only exist with certa phi and psi values | |
| in ramachandran plot for secondary structrues Unfavorable ones (i.e., steric crowding, white) • Favorable ones (i.e. H- bonding interactions, blue) | ok |
| structural asymmetry causes differences in the absorption of left- handed versus right- handed circularly polarized light. canbe used to assess secondary structure and to monitor protein folding. | circular dichroism (CD) analysis for secondary structure |
| Three-dimensional arrangement of all atoms in a protein. v Three-dimensional condensing of all secondary structural elements. | tertiary structure |
| 2 major classes of tertiary structure:________ proteins: long strands or sheets_________ proteins": spherical or global shape | Fibrous; Globular |
| Repeat a single type of secondary structure. • High percentage of hydrophobic amino acids. • Insoluble in water. • Important sructural proteins. | tertiary structrure: fibrous proteins |
| Contain several types of secondary structure. • Important enzymes and regulatory proteins. o allows them to interact with other biomolecules n can be water soluble and lipid soluble (plasma membrane) | tertiary structure: globular proteins |
| The arrangement of two or more polypeptide chains (subunits) in 3-D complexes. | quaternary structure |
| 2 main methods to determine higher-order protein structures | x-ray crystallography and NMR spectroscopy |
| 1) Crystallize the protein 2)Blast with X-ray 3)Collect diffraction data 4) Construct a 3D arrangement of atoms | x-ray crystallography |
| pros and cons of x ray crystallography? | pros - no size limits, high resolution cons - proteins must be able to crystallize, structure may stay the same |
| 1)Dissolve the protein 2) Collect NMR data 3) Assign NMR signals 4) Calculate the structure | NMR spectroscopy |
| pros and cons of NMR spec? | Pros: No need to crystallize the protein; motional dynamics of whole molecule. Cons: only suitable for small proteins |
| chapter 4 problem 7 | IN NOTES LECTURE 9 BIOCHEM |
| for beta turns, _______ is preferred as the turn because it is easier to turn as cis rather than trans | proline |
| when an amino acid is More________ in hydropathy, more likely it interacts with water well | negative |
| term for protein balance | proteostasis; like homeostasis but for proteins |
| misfolded proteins _______ | aggregate |
| proteostasis pathways? | synthesis --> folding --> unfolding --> misfolded, aggregates --> remodling --> degradation |
| Most proteins must maintain conformational flexibility in order to function. v The native structure is__________ most favorable, but also only marginally stable. | thermodynamically |
| Protein folding is a fast process. Sometimes protein folding happens spontaneously. More often it occurs with the assistance of specialized enzymes and complexes called________ . | chaperones |
| proteins that Interact with partially folded or misfolded polypeptides and facilitate correct folding. | chaperone proteisn |
| chaperone proteins are present in organisms franging from bacteria to humans. they require energy in the form of _______ to function because thermodynamic prefers randomness, and going from misfolded to a more organized correct fold requires energy | ATP |
| 2 major families of chaperone proteins: 1) ________ - prevent misfolding 2) _________ facilitate folding | Hsp70 and Chaperonins |
| loss of a protein's 3D structure | denaturation |
| when a protein loses its 3D structure it doesnt carry out the biological function T or F | true |
| denaturation: Unfolding is________ (loss of 3D-structure in one part destabilizes other parts). Most proteins can be denatured by heat. • ______ ________ (Tm): midpoint of the range of denaturing temperatures. 50% of protein is unfolded here | cooperative; Melting temperature |
| how could circular dichroism be used to monitor signals of protein denaturation? | CD • Has the alpha helix, beta conformation, and random coil • Change structure (no longer alpha, beta, or something) change in Beta conformation is different (or whatever your secondary structure is) |
| 5 denaturants | heat, extremes of pH, miscible organic solvents, solutes, detergents |
| -Heat disrupts____-bonds. - Extremes of pH disrupt______ interactions and ______-bonds. Miscible organic solvents (i.e. alcohol or acetone) disrupt________ interactions. | - hydrogen; ionic (alter pH, alter charge); hydrogen; hydrophobic |
| _______(i.e., urea) disrupt hydrophobic interactions and H-bonds. § _______ disrupt hydrophobic interactions. | Solutes; Detergents |
| chapter 4 probelm #4 in lecture 9 computer notes | |
| when you remove a denaturing agent, the protein spontaneously refolds into the _______ conformation and regains function | native |
| organelle that is major consumer of cellular oxygen | mitochondria |
| o to go through ETC,_______ is the final electron acceptor o ATP mainly produced through ETC and mitochondria and oxygen helps create_______ gradient | oxygen; proton |
| o Proton gradient is like a________ ♣ When it goes form intermembrane space to membrane ATP synthase turns and connects ADP and phosphate | turbine - lecture 9/13 page 4 |
| WHY WE NEED OXYGEN, MITOCHONDRIA, ETC, FOR COMPLEX___ IN ETC – COMPLEX USES OXYGEN HAS ELECTRON ACCEPTOR, NEED PROTON GRADIENT TO PRODUCE ATP Enzyme for complex is cytochrome c oxidase - forms water | FOUR |
| • Oxygen is critical but has________ water solubility and most chemical rxns occur in aqueous environment | poor |
| oxygen supply issues: | poor water solubility - can't ge carried to tissues in sufficient quantitiy and ineffective diffusion over long distance in larger multicellular animals |
| what oxygen binding proteins? A) transports oxygen; tetramer B) stores oxygen; monomer | A) hemoglobin B) myoglobin |
| protein family involved in oxygen binding proteins are ______ | globins |
| globin that is a monomer, protect neurons from hypoxia and ischemia | neuroglobin |
| globin who is a monomer and function is unknown | cytoglobin |
| hemoglobin and myoglobin are the most-studied/best-understood proteins. they are first ones with 3D structures determined. they are ______ proteins, so their tertiary structure contains several types of secondary structure; important enzymes/regulatory | globular |
| hemoglobin and myoglobin - examples ofr how other proteins work: a. ________ interactions with other molecules. b. ______ – conformational changes essential for function. c. ________ binding – specific and reversible. | Dynamic; Flexible; Ligand |
| Hemoglobin and myoglobin are________ proteins (conjugated proteins with the bound prosthetic group heme). | heme |
| protoporphyrin IX with a bound iron (Fe2+). | heme |
| Heme:________ oxygen binding. key function | reversible |
| true or false: None of the amino acid side chains can bind oxygen. | true |
| Transition metals such as____ and ______r have a strong tendency to bind oxygen. Free iron is highly reactive& generates ____ _____ ______(ROS) that damage macromolecules. | iron and coppe; reactive oxygen species |
| Heme: binds and transports oxygen without excessive amount of______. | ROS - reactive oxygen species (damage macromolecules) |
| ‘Free’ heme molecule leaves the Fe2+ with two _____ ______ bonds that can react with oxygen. • Once the Fe2+ is oxidized to Fe3+, heme can no longer bind oxygen. | ‘open’ coordination |
| Proteins sequester heme molecules deep inside the structure to prevent Fe2+________. | oxidation |
| protein that Stores O2 in muscles for metabolism. | myoglobin |
| myoglobin structure is Eight __--______segments connected by β–turns. there is______ heme per molecule | α-helical ; One |
| _______ is a ligand for myoglobin. • Myoglobin binds oxygen at the specific binding site. • Same applies to hemoglobin, except that the binding is more complex. | O2 |
| a molecule that binds (typically a small molecule). | ligand |
| a region in the protein where the ligand binds. | binding site |
| Ligand binds to the protein via ____-_______ forces – transient and reversible interactions. | non-covalent |
| ________expression describes the reversible binding of a ligand (L) to a protein (P): | Equilibrium; P + L ⇌ PL |
| chapter 5 problem 1 | |
| association and disassociation constant for ligand and protein | Ka = [PL]/[P][L] Kd = 1/Ka |
| fraction of ligand- binding sites on the protein that are occupied by ligand. ____ = [PL]/([PL] +[P]) | θ(theta) |
| Kd = _____when θ= 0.5; θ depends on the free [ligand] and Kd; | [L] ; θ = [L]/[L]+Kd |
| The fraction of bound sites θ depends on: 1) the____ ______ concentration, and 2) ________ | free ligand; Kd - disassociation constant |
| if one protein has a higher association constant for a ligand, (Ka) , than another protein, what does that mean? | the one with the higher association constant has a higher affinity for the ligand |
| for ligand analysis, the smaller the disassociation constant, the ________ the affinity | higher |
| practice problems lecture 09/15 from galina's notes page 4 and page 6 with myoglobin | ok |
| is this strong or week binding strength? Kd<10 nM | strong |
| is this weak or strong binding strength? Kd> 10 μM | weak |
| ________motions (“breathing”) produce transient cavities in myoglobin for oxygen to move in and out. • The distal His (His E7 or His64) facilitates O2 binding by forming a hydrogen bond. | Molecular |
| in equation for binding of O2 to myoglobin - The _____ _______of oxygen (pO2) is used in place of [O2], because [O2] is proportional to pO2. | p artial pressure |
| theta for fraction of ligand binding sites that are occupied by ligand for O2 to myoglobin is what | θ = pO2/pO2+Kd |
| Mb is relatively insensitive to change in O2 concentration/ pressure. if pO2 in tissues is about 4 kPa and the pO2 in lungs is about 13 kPa, can myoglobin be a good O2 transporter? | its good for O2 storage but not O2 transport because its theta is still about 1 fro 4 kPa and will not release the oxygen |
| Effective O2 Transport Requires ____-Dependent Affinity | pO2 |
| _______(cooperative) binding curve- more sensitive to small differences in O2 | Sigmoid |
| there can be _____ oxygens per hemoglobin | 4 |
| hemoglobin is a tetramer of two subunits (α2β2). α and β______ form a dimer.Tetramer is a dimer of αβ dimers. | protomers; |
| Hemoglobin in________ (red blood cells) binds and carries nearly all the O2 in the whole blood. these cells transport O2 | erythrocytes |
| Formed from hemocytoblasts (precursor stem cells) Incomplete, vestigial cells without intracellular organelles. life spand 120 days and main fucntion is to carry hemoglobin | erythrocytes |
| myoglobin is a monomers, so can it have quaternary structure? | no |
| each subunit of hemoglobin is_______ to myoglobin in 3D structure; alpha helix with beta turn and heme in the middle that binds oxygen | similar |
| there is a low identical sequence between alpha and beta subunits in hemoglobin, and there is no D-helix in alpha subunit, but in the Heme binding pocket: ___ and _____ helices in both subunits. | E and F |
| what are the subunit interactions in hemoglobin for the 4 subunits (alpha 1, alpha 2, beta 1, beta 2 = tetramer) | hydrophobic, hydrogen bonds, and ionic interactions |
| 2 major conformations for hemoglobin | tense state and relaxed state |
| predominant conformation of deoxyhemoglobin. | tense state |
| hemoglobin conformation that has a higher affinity for O2 than the T state. central cavity is collapsed and binds oxygen | relaxed state |
| • T state conformation • Large central cavity • Low affinity for O2 what state of hemoglobin? | apo state |
| • R state conformation • Collapsed central cavity • High affinity for O2 what state of hemoglobin? | saturated state |
| _____ binding triggers the tense state to relaxed state transition lecture 09/18 slide 2 figure | oxygen |
| hemoglobin: 1st O2 moleculebinds weakly to a subunit in the____- affinity T state. undergoes a transition from T state to the_____- affinity R state. More O2 molecules bound to the R state, making hemoglobin an ______ protein | low; high; allosteric |
| o Upon binding of first oxygen and the rest of the hemoglobin affinity of oxygen is_______ | increased |
| cooperative ligand binding - hill equation in lecture 11 notebooks | |
| (slope of Hill plot, degree of interaction): nH | Hill coefficient |
| Hill coefficient values and ligand binding co- operativity: nH = 1: ______ nH>1:_______ nH<1: _______ | none - binding of first ligand has no effect on binding of the rest of ligands; positive - first ligand binding has low affinity, but once first is bound, affinity increases ; negative - binding of first causes low affinity for others to bind |
| in an allosteric protein (like hemoglobin), A protein with_______ binding sites. • Binding sites/subunits______ with each other. Associated with ligand binding-induced _______ change. | multiple; interact; conformational |
| first binding event increases affinity at remaining sites. | positive cooperatity - nH > 1 |
| first binding event reduces affinity at remaining sites. | negative cooperativity - nH< 1 |
| Positive co-operativity can be recognized by_______ binding curves. | sigmoidal |
| Tissues generate CO2 from cellular respiration. Carbonic anhydrase catalyzes: CO2 + H2O--> H+ + HCO3−. INCREASE IN H+, LOWER PH, MORE ACIDIC, ______ O2 BINDING BY HEMOGLOBIN | DECREASES |
| Hb also carries 15-20% of the CO2 to the lungs and kidneys to be excreted. CO2 binds to the amino terminal in the form of a carbamate, stabilizes the T state, and promotes O2______. | dissociation |
| the effect of pH and [CO2]/pCO2 on the binding and release of O2 by Hb. high oxygen, Hb binds O2 and releases H+. low oxygen (tissue), hemoglobin binds H+ and releases O2 | bohr effect |
| o When pH is_____, the hemoglobin has lower affinity for oxygen releases oxygen o pH is_____, binds more oxygen | lower; higher |
| when pH jumps from 7.4 to 7.2 what is the impact on affinity of hemoglobin for oxygen? | pH is lower, theta is lower, hemoglobin has a decreased affinity for oxygen |
| chapter 5 problems 3a and 3B in lecture 11 notes | |
| intermediate in glycolysis, Polyanion, high in erythrocytes. LECTURE 09/18 PAGE 5 | 2,3-BPG |
| 2,3-BPG _____ hemoglobin affinity for O2; binds to hemoglobin (one per tetramer) and stabilizes the tense state. it ensures tissue oxygen delivery at high altitide | reduces |
| chapter 5 problem 3a,3b,3c lecture 11 | |
| CO fits in the same binding site as O2. • CO binds Hb 250 times better than O2. • CO is highly toxic. It blocks the function of myoglobin, hemoglobin, and others. | CO poisioning |
| carbon monoxide increases affinity for oxygen, but binds it so tight it doesn't release. true or false | true |
| • Life-threatening. • Individuals homozygous for the sickle-cell allele of the gene encoding Hb β subunit. • Normal Hb (Hb A) remains soluble upon deoxygenation. Mutated deoxygenated Hb (Hb S) forms insoluble fiber. | sickle cell anemia |
| sickle cell - Genetic disease: homozygous for Glu6 to Val6 mutation in Hb β chain. • Mutation creates a______ patch on the surface of deoxyhemoglobin S. bc globular, no longer charged AA on outsiide makes it curve inward | hydrophobic |
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