biochem test 1
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
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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. | show 🗑
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| biochem is the chemistry of what? | show 🗑
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| show | true
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| Glycolysis, an almost________ central pathway of glucose metabolism. | show 🗑
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| show | conserved
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| biochemistry is _______ in our daily life | show 🗑
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| what 4 things does biochemistry impact? | show 🗑
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| show | LECTURE 1 ANSWER
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| show | complexity
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| living matter must be able to Extract, transform, and utilize______ from their environment for maintenance, regeneration, and function. | show 🗑
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| energy _______ and _______ keep organisms alive | show 🗑
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| show | 1) from sunlight - plants, green bacteria, cyanobacteria 2) from nutrients/fuels- animals and most bactiera
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| 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 | show 🗑
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| living matter - regulated interactions between individual components that are ______ and ________ ex: cell signaling map and brain signaling for movment | show 🗑
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| living matter - fairly _______ self replication (DNA) while allowing enough _____ for evolution. biological reproduction with near-perfect fidelity | show 🗑
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| show | prokaryotes: bacteria and archaea
eukaryotes: eukarya
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| show | elements --> monomers --> polymers --> supramolecular structures --> organelles --> cells --> tissues --> organisms
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| simple organic compounds | show 🗑
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| macromolecules | show 🗑
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| show | C, H, O, N, P, S
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| show | Na+, K+, Ca2+, Cl-
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| show | Mg++, Zn++, Fe++, Mn++, Cu++
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| show | nucleic acids
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| show | lipids
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| what simple organic compound? parent sugar is glucose | show 🗑
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| show | functional groups
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| GO OVER COMMON FUNCTIONAL GROUP FLASH CARDS HOE | show 🗑
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| interactions between biomolecules are _______ | show 🗑
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| show | specific; lock and key; stereospecific
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| show | Three-Dimensional
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| show | 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)
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| major macromolecules? (4) | show 🗑
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| show | monomeric units (nucleotides, amino acids, sugars) --> marcomolecules (DNA, protein, cellulose) --> supramolecular complexes (chromatin, plasma membrane, cell wall) --> cell/organelles
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| show | cells;single; origin, morphology, and function.
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| show | eukaryotes have nucleus, nuclear membrane, and membrane bound organelles and because of compartmentalization, they have spatial separation of energy yielding and energy consuming reactions
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| PROKARYOTE VS EUKARYOTE LECTURE 1 | show 🗑
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| show | chemical
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| 2 parts of metabolism? | show 🗑
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| 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 | show 🗑
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| show | anabolism
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| catabolic reaction pathways are _______ and anabolic reaction pathways are __________ | show 🗑
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| anabolic pathways proceed ________ with catabolic pathways in a dynamic steady state | show 🗑
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| show | oxidation of glucose (C6H12O6 + 6O2 --> 6CO2 AND 6H20
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| show | ATP; coenzymes ; lecture 2 page 1 catabolism
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| release of energy | show 🗑
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| show | phosphoanhydride bonds are high energy --> broken, energy released
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| . 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. | show 🗑
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| Cells are efficient_______ of energy (convert energy from one form to another) , capable of interconverting _____, ________, _______, and _______ energy with great efficiency. | show 🗑
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| show | ; convert
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| organisms perform energy ______ to accomplish work and stay alive | show 🗑
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| show | synthesize; Consume; reductive
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| “New formation of sugar” that converts pyruvate and related three- and four-carbon compounds to glucose. | show 🗑
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| in gluconeogenesis, Essentially same reactions in all tissues and all species. The_______ context and the________ of gluconeogenesis differ between species and tissues. | show 🗑
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| important gluconeogenesis precursors in animals? | show 🗑
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| show | endergonic
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| show | second law of thermodynamics
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| (the amount of energy capable of doing work during a reaction at constant temperature and pressure). | show 🗑
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| the heat content of the reaction system). | show 🗑
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| show | entropy (S)
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| show | negative (exergonic)
+∆S - increasing disorder; products more disordered than reaactants
-∆H - release heat
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| show | ∆G = ∆H - T∆S
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| _______ΔG: endergonic reaction that gains free energy. _______ ΔG: exergonic reaction that releases energy. | show 🗑
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| ü Endergonic ü ΔG > 0 ü Reactants are stable ü Reaction is not spontaneous | show 🗑
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| ü Exergonic ü ΔG < 0 ü Products are stable ü Reaction is spontaneous | show 🗑
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| Chemical________ of exergonic and endergonic reactions allows otherwise unfavorable reactions. • The “high-energy” molecule (______) reacts directly with the metabolite that needs “activation.” | show 🗑
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| A thermodynamically unfavorable (endergonic) reaction can be driven in the forward direction by coupling it to a thermodynamically favorable (exergonic) reaction through a_______ ________ | show 🗑
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| kinetics - intermediate between substrate and product;unstable; and distinct conformation. | show 🗑
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| show | activation energy
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| show | slower
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| show | equals; change
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| show | ΔG
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| show | EQUATION ON LECTURE 2 PAGE 5
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| For chemical reactions, ΔG'o is dependent on the ______ | show 🗑
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| show | favorable ; large Keq = favorable ∆G
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| show | forward
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| when Keq = 1, ∆G is zero, and starting with all components at 1 M the reaction is ___________ | show 🗑
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| when Keq <1, ∆G is positive and starting with all components at 1 M then the reaction proceeds _________ | show 🗑
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| 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. | show 🗑
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| show | Actual
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| show | -Higher temperatures (may destabilize macromolecules)
-Higher concentrations of reactants (need more
valuable starting material)
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| how to speed up reactions, that would work in living organisms? | show 🗑
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| Enzymes Lower the _____ ______ to Increase the Reaction Rate | show 🗑
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| LECTURE 2 NOTES - CHANGE REACTION BY COUPLING WITH A FAST ONE NOTES ! | show 🗑
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| show | miller and urey
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| show | 160,000 ; 350,000,000
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| show | water; aqueous; water
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| show | charged; polar
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| show | NONPOLAR
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| show | oxygen
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| show | amphipathic
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| show | CO2 - oxygen has poor solubility in water. O2 is very nonpolar, and so is CO2 but CO2 has some partial negative on the oxygens
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| show | Electronegativity
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| show | tetrahedron - 2 pairs bond to H and 2 lone pairs
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| show | 4; 2; energy to break H-bond vs energy to break the covalent O-H bond: 1:20
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| 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. | show 🗑
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| 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 | show 🗑
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| show | hydrogen, ionic, van der waals, hydrophobic
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| for hydrogen bonding you have to have an _______, and a _________. water can serve as both of these | show 🗑
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| show | direction and strength; straight - stronger, bent - weaker
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| show | charged; ion; dipole
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| ion-dipole interactions - Water is dipole that interacts electrostatically with charged solutes by orienting H toward______ and O toward______. | show 🗑
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| show | uncharged
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| show | van der waals
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| 2 components of van der waals? | show 🗑
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| show | attractive
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| van der waals (Steric repulsion) that dominates at short distance. | show 🗑
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| compounds that have hydrophilic group and hydrophobic group | show 🗑
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| show | aggregates
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| show | micelles
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| show | Weak - summary lecture 3
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| 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. | show 🗑
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| Properties such as viscosity, surface tension, taste, and color, etc. that depend strongly on the chemical nature of the solute. | show 🗑
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| Cytoplasm of cells are highly_______ solutions and have high_______ pressure. | show 🗑
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| the measure of solute concentration | show 🗑
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| show | Isotonic; Hypertonic; Hypotonic
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| 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 | show 🗑
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| what is wrong with this commonly seen formula? H2O --> H+ + OH- | show 🗑
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| show | proton hopping ; lecture 5 page 1
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| proton hopping applies to the hydroxyl ion in water, except in the ________ direction | show 🗑
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| constant that is a Fixed value that is characteristic for each specific reaction. concentration of products over reactants ; determined by electrical conductivity measurements | show 🗑
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| equilibrium constant for water? | show 🗑
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| Kw, ion product of water is equal to what? | show 🗑
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| at pH=7, the concentration of[H+] and [OH] are what? Kw = [H+][OH-]= 1 x 10^-14 M^2 | show 🗑
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| a mathematical term that means the negative log of. | show 🗑
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| pH = what mathematically? | show 🗑
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| show | 14
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| show | pH > 7
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| show | pH = 7
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| show | pH <7
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| show |
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| show | true
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| Strong Acid + Strong Base = ??? HCl + NaOH | show 🗑
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| show | weak acids
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| for weak acids, the extent of dissociation is ___-dependent | show 🗑
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| for weak acids: ow pH, high [H+] push the reaction to the______ very little of the weak acid will be dissociated into ions. | show 🗑
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| show | right; HA (equilibrium arrows) (H+) + (A-)
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| acid dissociation constant | show 🗑
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| show |
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| show | one half
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| when [A-] =[HA], then pH=? | show 🗑
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| LECTURE 5 PAGE 6 TITRATION | show 🗑
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| when pKa = pH, the weak acid is ______ dissasociated | show 🗑
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| 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 | show 🗑
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| show | stronger
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| show | acetic acid and acetate are conjugate acid/base pair; acetic acid is proton donor and acetate is proton acceptor
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| acid that gives up only one proton - CH3COOH(equilibrium arrows) H+ + CH3COO- | show 🗑
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| show | diprotic acid
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| acid that gives up three protons (H3PO4) | show 🗑
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| show | the first proton removal is always the strongest weak acid
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| Almost every biological process is_____- dependent. A small change in pH produces a______ change in the rate of the process. | show 🗑
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| show | cytosolic; buffers; constancy
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| aqueous systems that resist changes in pH when small amounts of acid (H+) or base (OH-) are added. | show 🗑
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| show | weak; conjugate base
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| show | buffering region
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| 2 important physiological buffers? | show 🗑
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| 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. | show 🗑
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| show | bicarbonate buffer; H2CO3 --> H+ + HCO3-
carbonic acid (H2CO3) is from dissovled CO2 and water
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| when the CO2 bicarbonate buffer system is disrupted, pH<7.35 and you get what condition? | show 🗑
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| show | proteins
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| show | diverse
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| show | amino acids
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| Proteins (from bacteria to human beings) are constructed from a common set of____ amino acids. | show 🗑
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| show | combinations and sequences.
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| show | proline is cyclic
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| show | organic nomenclature and biochemical designation
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| show | Organic; Biochemical
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| 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? | show 🗑
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| show | L, D
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| 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. | show 🗑
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| Cells use enzymes with_________ active sites to select L amino acids! | show 🗑
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| 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 | show 🗑
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| show |
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| show | uncommon amino acids
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| lecture 6 biochem page 6 post translational modification | show 🗑
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| in a reducing agent, a disulfide bond would be _______ in cystine to form 2 cysteine amino acids with sulflhydryl bonds | show 🗑
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| ionization of amino acids - At acidic pH, the______ group is protonated and the amino acid is in the cationic form. | show 🗑
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| show | deprotonated; protonated; Zwitterions
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| show | neutral
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| show | zwitterions - lectrue 6 page 6
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| show |
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| show | 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
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| Zwitterions_______ at pH values between the pKa values of the amino and carboxyl groups. | show 🗑
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| show | pI = Pk1 + pK2/ 2
the average of pK's
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| At the isoelectric point, AA: o net charge is_____ o ______ soluble in water o does not_____ in electric field | show 🗑
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| 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. | show 🗑
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| how do you calculate pI with more than 2 ionizable things in side chains? | show 🗑
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| at pH = 7 Aspartate and Glutamate are______ charged • Lysine and Arginine are________ charged • ________ may be positively charged or uncharged | show 🗑
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| show |
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| Peptides are chains of amino acids covalently joined through a substituted amide linkage, termed a _____ ______ | show 🗑
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| peptide bonds are formed from a __________ reaction | show 🗑
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| show | reactive; dipole; rigid; planar
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| show | double; chem 471 09_06 lecture page 1
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| in a peptide, which bonds can rotate? | show 🗑
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| show | N-terminal to C-terminal
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| show | answer in notes biochem lecture 6 and on laptop highlight
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| show | true ; Naturally occurring peptides range from 2 amino acid residues to many thousands. bioactive small peptides - hormones, pheromones, neuropeptides, toxins
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| terminology for few amino acids in a peptide | show 🗑
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| terminology for many amino acids in a peptide | show 🗑
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| generally, polypeptides have a molecular weight less than ???? and proteins have a molecular weight greater than ???? the average weight of an amino acid is ???? | show 🗑
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| proteins are made of polypeptides, but polypeptides are NOT made of protein. T or F | show 🗑
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| proteins may contain: a single polypeptide; two or more polypeptides held by both _______ and _________ interactions | show 🗑
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| show | Cofactors; Coenzymes; Prosthetic
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| show | conjugated proteins
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| ________group is the non-amino acid part of a conjugated protein. | show 🗑
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| show | amino acid sequence = identity).
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| show | DNA; mass
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| before sequencing a protein, what must be done first? | show 🗑
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| show | amino acid
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| show | oxidizing and reducing agents
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| show | chemical sequencing - edman degradation
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| what molecules are to be analyzed in mass spectroscopy? | show 🗑
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| show | mass spectroscopy
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| how does mass spectroscopy sequence proteins/peptides? | show 🗑
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| show | cardiolipin
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| when laying out a research plan, you want to monitor the _________ for all throughout the isolation process. (ex: change pH --> protein can change conformation) | show 🗑
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| in research plan: lyse cells /cell structure breaks apart = __________ separate organelles from cell debris/ separate soluble proteins from insoluble proteins = __________ | show 🗑
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| 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 ________ | show 🗑
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| 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 | show 🗑
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| separates substances based on density | show 🗑
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| show | supernatant - organelles
and pellet that contains whole cells, nuclei, cytoskeleton,e tc.
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| on high speed for centrifugation of homogenized tissue, there are what 2 main densities/ | show 🗑
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| how do you use centrifugation to separate organelles? aka separate mitochondria, lysosomes, peroxisomes etc after regular centrifugation? | show 🗑
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| how do you acquire soluble proteins in protein methods? lecture 09/08 page 3 | show 🗑
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| show | separation
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| show | stationary, mobile, effluent
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| solid porous matrix inside the column. what chromotagraphy phase? | show 🗑
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| show | mobile
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| the solution that comes out of the column, collected as fractions. what chromatagraphy phase? | show 🗑
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| Three Chromatographical Methods for Protein Purification: | show 🗑
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| 2 types of ion exchange chromatography | show 🗑
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| ion exchange chromatography - AnionExchange 1. Matrix (____) charged. 2. Proteins (____) bind. 3. Elution: High salt,________ conditions. | show 🗑
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| show | negative; positive; basic - negatively charged basic eludes and pulls positive proteins from negative matrix
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| show | negative
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| ch 3 problem 17 | show 🗑
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| show | first; last ; smaller can get stuck in matrix and larger cannot
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| chromatography where separation by binding specificties between ligand and a protein | show 🗑
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| show | 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
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| show | dialysis
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| show | hinders; conducts
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| show | from negative to positive
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| 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 | show 🗑
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| what does SDS page do to a protein? | show 🗑
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| show | distance traveled on gel/total gel length
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| PROTEIN METHODS - ESTIMATE MW BY SDS PAGE LOOK AT lecture 09/08 | show 🗑
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| what are the 2 dimensions in 2D electrophoresis? | show 🗑
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| show | ok
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| show | isoelectric points.; zero
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| Protein molecules adopt a specific 3-dimensional conformation (called the _____ _______). this conformation is mainly held together by favorable_________ interactions. | show 🗑
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| show | energy
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| protein structure: AA sequence that determines function | show 🗑
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| protein structure: Local folding: α-helix, β-sheet, random coil | show 🗑
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| protein structure: “Global” folding of a single polypeptide chain | show 🗑
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| proteins tructure: Subunit arrangement: assembly of folded proteins into multi-subunit macromolecules– dimer, trimer, tetramer, etc. | show 🗑
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| show | no - bc it doesn't have multiple subunits
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| show | covalently
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| 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 | show 🗑
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| show | alpha helix
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| 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 | show 🗑
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| show | α helix ; dipole between N+ and O-...
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| show | Sequence
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| show | small hydrophobic
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| show | Pro; Gly
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| why can't proline rotate well? | show 🗑
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| show | apices; alternate; pleat
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| what secondary structure for protein? -Peptide chains align side-by-side. -Interstrand H-bond-Parallel and Antiparallel | show 🗑
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| show | parallel and antiparallel
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| show | beta turn
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| _______ or _______ residues are commonly found in beta turns | show 🗑
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| type I beta turn: | show 🗑
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| type 2 beta turn: | show 🗑
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||||
| type 1 beta turns occurs _____ times more frequently than type 2 | show 🗑
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||||
| for type 1 and 2 beta turns, why can't glycine or proline be in 1 or 2 AA position? | show 🗑
|
||||
| show | trans
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|
||||
| Peptide conformation is defined by dihedral angles (or torsion angles). Dihedral angles: o Φ (phi): what angle? ψ (psi): ? | show 🗑
|
||||
| show |
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|
||||
| in ramachandran plot for secondary structrues Unfavorable ones (i.e., steric crowding, white) • Favorable ones (i.e. H- bonding interactions, blue) | show 🗑
|
||||
| show | circular dichroism (CD) analysis for secondary structure
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|
||||
| show | tertiary structure
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|
||||
| 2 major classes of tertiary structure:________ proteins: long strands or sheets_________ proteins": spherical or global shape | show 🗑
|
||||
| show | tertiary structrure: fibrous proteins
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||||
| show | tertiary structure: globular proteins
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|
||||
| The arrangement of two or more polypeptide chains (subunits) in 3-D complexes. | show 🗑
|
||||
| show | x-ray crystallography and NMR spectroscopy
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|
||||
| show | x-ray crystallography
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|
||||
| show | pros - no size limits, high resolution
cons - proteins must be able to crystallize, structure may stay the same
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|
||||
| 1)Dissolve the protein 2) Collect NMR data 3) Assign NMR signals 4) Calculate the structure | show 🗑
|
||||
| show | Pros: No need to crystallize the protein; motional dynamics of whole molecule.
Cons: only suitable for small proteins
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|
||||
| show | IN NOTES LECTURE 9 BIOCHEM
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|
||||
| show | proline
🗑
|
||||
| when an amino acid is More________ in hydropathy, more likely it interacts with water well | show 🗑
|
||||
| term for protein balance | show 🗑
|
||||
| misfolded proteins _______ | show 🗑
|
||||
| show | synthesis --> folding --> unfolding --> misfolded, aggregates --> remodling --> degradation
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|
||||
| show | thermodynamically
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|
||||
| show | chaperones
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|
||||
| proteins that Interact with partially folded or misfolded polypeptides and facilitate correct folding. | show 🗑
|
||||
| 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 | show 🗑
|
||||
| show | Hsp70 and Chaperonins
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|
||||
| show | denaturation
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|
||||
| when a protein loses its 3D structure it doesnt carry out the biological function T or F | show 🗑
|
||||
| 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 | show 🗑
|
||||
| how could circular dichroism be used to monitor signals of protein denaturation? | show 🗑
|
||||
| show | heat, extremes of pH, miscible organic solvents, solutes, detergents
🗑
|
||||
| show | - hydrogen; ionic (alter pH, alter charge); hydrogen; hydrophobic
🗑
|
||||
| _______(i.e., urea) disrupt hydrophobic interactions and H-bonds. § _______ disrupt hydrophobic interactions. | show 🗑
|
||||
| chapter 4 probelm #4 in lecture 9 computer notes | show 🗑
|
||||
| show | native
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|
||||
| organelle that is major consumer of cellular oxygen | show 🗑
|
||||
| o to go through ETC,_______ is the final electron acceptor o ATP mainly produced through ETC and mitochondria and oxygen helps create_______ gradient | show 🗑
|
||||
| show | turbine - lecture 9/13 page 4
🗑
|
||||
| show | FOUR
🗑
|
||||
| • Oxygen is critical but has________ water solubility and most chemical rxns occur in aqueous environment | show 🗑
|
||||
| show | poor water solubility - can't ge carried to tissues in sufficient quantitiy and ineffective diffusion over long distance in larger multicellular animals
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|
||||
| show | A) hemoglobin
B) myoglobin
🗑
|
||||
| protein family involved in oxygen binding proteins are ______ | show 🗑
|
||||
| show | neuroglobin
🗑
|
||||
| globin who is a monomer and function is unknown | show 🗑
|
||||
| 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 | show 🗑
|
||||
| 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. | show 🗑
|
||||
| show | heme
🗑
|
||||
| protoporphyrin IX with a bound iron (Fe2+). | show 🗑
|
||||
| Heme:________ oxygen binding. key function | show 🗑
|
||||
| show | true
🗑
|
||||
| Transition metals such as____ and ______r have a strong tendency to bind oxygen. Free iron is highly reactive& generates ____ _____ ______(ROS) that damage macromolecules. | show 🗑
|
||||
| Heme: binds and transports oxygen without excessive amount of______. | show 🗑
|
||||
| show | ‘open’ coordination
🗑
|
||||
| show | oxidation
🗑
|
||||
| protein that Stores O2 in muscles for metabolism. | show 🗑
|
||||
| show | 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. | show 🗑
|
||||
| show | ligand
🗑
|
||||
| a region in the protein where the ligand binds. | show 🗑
|
||||
| show | non-covalent
🗑
|
||||
| ________expression describes the reversible binding of a ligand (L) to a protein (P): | show 🗑
|
||||
| chapter 5 problem 1 | show 🗑
|
||||
| show | Ka = [PL]/[P][L]
Kd = 1/Ka
🗑
|
||||
| show | θ(theta)
🗑
|
||||
| show | [L] ; θ = [L]/[L]+Kd
🗑
|
||||
| The fraction of bound sites θ depends on: 1) the____ ______ concentration, and 2) ________ | show 🗑
|
||||
| show | 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 | show 🗑
|
||||
| practice problems lecture 09/15 from galina's notes page 4 and page 6 with myoglobin | show 🗑
|
||||
| is this strong or week binding strength? Kd<10 nM | show 🗑
|
||||
| is this weak or strong binding strength? Kd> 10 μM | show 🗑
|
||||
| show | Molecular
🗑
|
||||
| show | p artial pressure
🗑
|
||||
| theta for fraction of ligand binding sites that are occupied by ligand for O2 to myoglobin is what | show 🗑
|
||||
| show | 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
🗑
|
||||
| show | pO2
🗑
|
||||
| show | Sigmoid
🗑
|
||||
| there can be _____ oxygens per hemoglobin | show 🗑
|
||||
| hemoglobin is a tetramer of two subunits (α2β2). α and β______ form a dimer.Tetramer is a dimer of αβ dimers. | show 🗑
|
||||
| Hemoglobin in________ (red blood cells) binds and carries nearly all the O2 in the whole blood. these cells transport O2 | show 🗑
|
||||
| Formed from hemocytoblasts (precursor stem cells) Incomplete, vestigial cells without intracellular organelles. life spand 120 days and main fucntion is to carry hemoglobin | show 🗑
|
||||
| show | no
🗑
|
||||
| show | similar
🗑
|
||||
| show | E and F
🗑
|
||||
| what are the subunit interactions in hemoglobin for the 4 subunits (alpha 1, alpha 2, beta 1, beta 2 = tetramer) | show 🗑
|
||||
| 2 major conformations for hemoglobin | show 🗑
|
||||
| predominant conformation of deoxyhemoglobin. | show 🗑
|
||||
| show | relaxed state
🗑
|
||||
| show | apo state
🗑
|
||||
| show | saturated state
🗑
|
||||
| show | 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 | show 🗑
|
||||
| show | increased
🗑
|
||||
| show |
🗑
|
||||
| show | Hill coefficient
🗑
|
||||
| Hill coefficient values and ligand binding co- operativity: nH = 1: ______ nH>1:_______ nH<1: _______ | show 🗑
|
||||
| in an allosteric protein (like hemoglobin), A protein with_______ binding sites. • Binding sites/subunits______ with each other. Associated with ligand binding-induced _______ change. | show 🗑
|
||||
| first binding event increases affinity at remaining sites. | show 🗑
|
||||
| first binding event reduces affinity at remaining sites. | show 🗑
|
||||
| show | 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 | show 🗑
|
||||
| show | 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 | show 🗑
|
||||
| o When pH is_____, the hemoglobin has lower affinity for oxygen releases oxygen o pH is_____, binds more oxygen | show 🗑
|
||||
| show | pH is lower, theta is lower, hemoglobin has a decreased affinity for oxygen
🗑
|
||||
| show |
🗑
|
||||
| show | 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 | show 🗑
|
||||
| chapter 5 problem 3a,3b,3c lecture 11 | show 🗑
|
||||
| show | CO poisioning
🗑
|
||||
| carbon monoxide increases affinity for oxygen, but binds it so tight it doesn't release. true or false | show 🗑
|
||||
| show | sickle cell anemia
🗑
|
||||
| show | hydrophobic
🗑
|
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