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EK Bio 1
molec bio + cellular respiration
| Question | Answer |
|---|---|
| hydrogen bonding in water allows.. | it to maintain liquid state in the cellular environment |
| lipids | any biological molecule that has low solubility in water and high solubility in nonpolar organic solvents; hydrophobic |
| what are the six groups of lipids? | fatty acids, triacylglycerols, glycolipids, terpenes, steroids, phospholipids |
| fatty acids | building blocks of most complex lipids; long chains of carbons with carboxylic acid at one end |
| triacylglycerols | aka triglycerides (fats and oils) constructed from three C glycerol with having a carbon chain; STORE ENERGY AND PROVIDE THERMAL INSULATION AND PADDING |
| phospholipids | built from glycerol backbone but a SERVE AS STRUCTURAL COMPONENT OF MEMBRANES; polar phosphate replaces one of the fatty acids to create an amphipathic molecule |
| steroids | four ringed structures that include hormones, vitamin D, and cholesterol (also membrane component); REGULATE METABOLIC ACITIVITIES |
| eicosanoids | SERVE AS LOCAL HORMONES; include prostaglandins, thromboxanes, and leukotrienes |
| proteins | built from a chain of amino acids linked together by peptide bonds |
| essential amino acids | humans have 10 - meaning humans cannot manufacture these 10 and must be ingested |
| non polar R groups | glycine, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan, methionine, proline |
| polar R groups | serine, threonine, cysteine, tyrosine, asparagine, glutamine |
| acidic R groups | aspartic acid, glutamic acid |
| basic R groups | lysine, arginine, histidine |
| primary structure | number and sequence of amino acids in polypeptide chain |
| secondary structure, alpha helix and beta pleated sheets | contribute to conformation of protein |
| alpha helix | conformation of single protein chain (twisted into helix) which are reinforced by hydrogen bonds between carbonyl oxygen and hydrogen on amino group |
| beta pleated sheet | connecting segments of two strands of sheet can lie parallel or anti-parallel which are reinforced by hydrogen bonds between carbonyl oxygen and hydrogen on amino group |
| tertiary structure | 3D shape of peptide chain created by (1) covalent disulfide bonds between 2 cysteine (2) electrostatic interactions btw acidic and basic side chains (3) hydrogen bonds (4) VDW forces (5) hydrophobic side chains pushed away from H2O |
| quaternary structure | shape when two or more polypeptide chains bind together, depends on same five forces that tertiary structure does |
| globular proteins | function as enzymes, hormones, membrane pumps and channels, membrane receptors, intercellular and intracellular transport and storage, osmotic regulators, immune response - antibodies |
| structural proteins | made of long polymers which maintain and add strength to cellular and matrix structure (collagen, microtubules) |
| glycoprotein | proteins w/ carb groups attached |
| cytochromes | proteins which require prosthetic heme grope in order to function |
| carbohydrates | aka sugars or saccharides, made of carbon and water |
| glucose | 6 carbon carb, most commonly occurring, accounts for 80% of carbs absorbed by humans, exists in aqueous sol'n favoring ring form |
| alpha-glucose | OH group on anomeric carbon (Carbon 1) and the methoxy group (Carbon 6) are on opposite side of carbon ring |
| beta-glucose | OH group and CH3OH group are on the same side |
| glycogen | alpha linked polymerized glucose found in all animal cells as a way to store glucose |
| starch | another alpha linked glucose, comes in two forms amylose and amylopectin |
| cellulose | beta linked polymerized glucose, animals cannot digest beta linkages only bacteria can digest |
| nucleotide | composed of a five carbon sugar, nitrogenous base, and a phosphate group |
| most common nitrogenous bases | adenine, guanine, cytosine, thymine, and uracil |
| phosphodiester bond | joins the nucelotides by creating bond between phosphate group of one nucleotide and the 3rd carbon of the pentose of the other nucelotide |
| adenine and thymine form how many H bonds | two |
| cytosine and guanine form how many H bonds | three |
| ATP | adenosine triphosphate, nucleotide that acts as source of readily available engery for the cell |
| cAMP | cyclic AMP, important component of second messenger systems |
| coenzymes involved in the Kreb's cycle | NADH and FADH2 |
| minerals | dissolved inorganic ions inside and outside the cell; assist in transport of substances entering/exiting cell; can combine and solidify to give strength to matrix; can act as co-factors assisting enzyme or protein function |
| enzymes | globular protein, function as catalyst to lower energy of activation for bio rxn and increasing rate of rxn; exhibit saturation kinetics |
| lock and key theory | active site of the enzyme has a specific shape like a lock that only fits a specific substrate (the key) |
| induced fit enzyme model | the shape of both the enzyme and substrate are altered upon binding which increases specificity and helps rxn to proceed; in cases with multiple substrates, the enzyme can orient substrates relative to each other to create optimal conditions for the rxn |
| saturation kinetics | where as the relative concentration of substrate increases, the rate of rxn also increases, but to a lesser and lesser degree until a max rate has been achieved |
| factors affecting enzyme rxns | substrate conc, temp, pH, cofactors |
| cofactor | non-protein component required by enzymes to reach optimal activity (coenzymes or metal ions) |
| coenzyme | organic molecules that help enzymes obtain optimal activity; divided into two types - cosubstrates and prosthetic; eg: vitamins |
| cosubstrate | reversibly bind to specific enzyme & transfer some chem group to another substrate and reverted back to original by another enzymatic reaction; eg: ATP |
| prosthetic group | remain covalently bound to enzyme through reaction; eg: heme |
| temperature and enzymatic rxns | increased temp will increase rxn rate until enzyme is denatured, then it rxn rate drops dramatically |
| pH and enzymatic rxns | optimal pH depends on enzyme |
| types of enzyme inhibition | irreversible, competitive, non-competitive |
| irreversible inhibitor | agent that binds covalently to enzymes to disrupt their function; tend to be highly toxic |
| competitive inhibitor | agents which compete with the substrate by binding reversibly with noncovalent bonds to the active site, can be overcome with increasing the substrate concentration, raises apparent Km but Vmax remains same |
| noncompetitive inhibitor | agents which bind noncovalenty to an enzyme at a spot other than the active site and change the confirmation of enzyme, will lower Vmax but the affinity of the enzyme remains the same (Km) |
| Km | Michealis constant, substrate conc at which the rxn rate is equal to 1/2 the Vmax, good indicator of enzyme's affinity to substrate |
| four methods of enzyme regulation | proteolytic cleavage, reversible covalent modification, control proteins, allosteric interactions |
| proteolytic cleavage | enzymes become irreversibly active when after specific peptide bonds cleaved on its zymogen/proenzyme |
| reversible covalent modification | activated/deactivated by phosphorylation or addition of some other modifier (often accomplished by hydrolysis) |
| control proteins | protein subunits that associate with certain enzymes to activate/inhibit their activity; eg calmodulin or G-proteins |
| allosteric regulation | molecules that regulate enzyme activation/inhibition by causing conformational change (eg feedback inhibition); not necessarily noncompetitive inhibitors; exhibit atypical kinetics |
| negative feedback | one of the products downstream inhibits the enzyme early in the reaction |
| positive feedback | one of the products returns to activate the enzyme (occurs less often then negative) |
| positive cooperativity | after the first substrate changes the shape of the enzyme, the other substrates bind more easily (like oxygen on hemoglobin) |
| categories of enzymes | oxidoreductases, transferases, hydrolyses, lyases, isomerases, ligases |
| metabolism | all cellular chemical rxns consisting of anabolism (molecular synthesis) and catabolism (molecular degradation) |
| three stages of metabolism | (1)macromolecules broken down to their constituent parts (2)constituent parts oxidized to acetyl CoA/pyruvate/other metabolite forming some ATP and reduced coenzymes(no O2) (3)if O2 available, metabolites go into citric acid cycle & oxidative phosphor |
| respiration | energy acquiring stages of metabolism, can be anaerobic or aerobic |
| anaerobic respiration | respiration where oxygen is not required, includes glycolysis and fermentation |
| glycolysis | series of rxns that breaks 6-C glucose molecule into two 3-C molecules of pyruvate |
| 6-C stage of glycolysis | expends two ATPs to phosphorylate the molecule |
| 3-C stage of glycolysis | synthesizes 2 ATP with each 3 carbon molecule |
| glycolysis products | 4 ATP + 2 pyruvate + 2 NADH |
| glycolysis reactants | glucose + 2 ATP + 2 NAD+ |
| glycolysis reaction | glucose + 2 ATP + 2 NAD+ --> 2 pyruvate + 4 ATP + 2 NADH |
| irreversible steps of glycolysis | (1) glucose to glucose-6-phosphate (phosphorylated glucose) - assists facilitated diffusion mech which transports glucose into the cell (2) fructose-6-phosphate to fructose-1,6-bisphosphate at the expense of ATP |
| substrate level phosphorylation | formation of ATP from ADP and inorganic phosphate using the energy released from the decay of high energy phosphorylated compounds as opposed to using the energy from diffusion) |
| fermentation | glycolysis + reduction of pyruvate to etOH or lactic acid + oxidation of NADH back to NAD+ |
| when does fermentation take place | when cell/organism either unable to use the energy from NADH and pyruvate or has no oxygen to do so |
| why does NAD+ need to be restored (in fermentation) | NAD+ acts as a coenzyme in glycolysis |
| where does glycolysis take place | cytosol |
| aerobic respiration | requires oxygen, produces 36 net ATP (including glycolysis) |
| NADH brings back how many ATP | 2 - 3 |
| FADH2 brings back how many ATP | 2 |
| Kreb's cycle | aka citric acid cycle, takes place in mitochondrial matrix to produce 1 ATP, 3 NADH, and 1 FADH2 (also substrate level phosphorylation), loses two carbons as CO2, and reproduces oxaloacetic acid |
| Acetyl CoA | coenzyme which transfers 2 carbons from pyruvate to the 4-C oxaloacetic acid to begin the Kreb's cycle |
| fatty acids role in respiration | tryglyceride - glycerol converted to PGAL and fatty acids converted go acyl CoA to acetyl CoA |
| proteins role in respiration | deaminated in liver so amino acids can be converted to pyruvic acid or acetyl CoA or other steps in the Kreb's cycle |
| electron transport chain | series of proteins (including cytochromes with heme) in the membrane of mitochondrion where electrons are passed down to ultimately be accepted by oxygen to create a proton gradient |
| oxidative phosphorylation | producing ATP using a proton motive force pushing protons through ATP synthase |
| overall respiration rxn | glucose + O2 --> CO2 + H20 |
Created by:
miniangel918
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