ACS Biochemistry Final – Flashcards

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pKa (chapter 3)
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measure of the tendency of a group to give up a proton (acidity); tendency decreases tenfold as pKa increases by one unit
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thioester bond (1)
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compounds with functional group C-S-CoA-C (eg, in acetyl-CoA)
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zwitterion (3)
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dipolar ion with both positive and negative groups but overall neutral charge; can act as either an acid or base
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Isoelectric point (pI) (chapter 3)
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the characteristic pH at which the net electric charge is zero
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SDS - Sodium Dodecyl Sulfate (chap 3)
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detergent used to unfold proteins and give them uniform negative charge
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SDS Page (3)
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chromatography used to separate proteins based on mass. light proteins travel fast than heavier ones
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PCR - Polymerase chain reaction (3)
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copies DNA multiple times to increase sample size
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Isoelectric focusing (chapt 3)
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procedure used to determine the isoelectric pt (pI) of a protein. Protein migrates through gel until pH = pI (net charge = 0)
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Two-Dimensional Electrophoresis (3)
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combines isoelectric focusing and SDS electrophoresis; separates proteins by both molecular weight and pI
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specific activity (3)
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number of enzyme units per mg of total protein (a measure of enzyme purity)
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activity (3)
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total units of a certain enzyme in a solution
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Peptide bonds (chapter 4)
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C-N bond with double bond character due to resonance (C-N bond cannot rotate, and is planar)
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Edman degredation (3)
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used in the sequencing of polypeptides; labels and removes ONLY the amino-residue from a polypeptide. carried out in a machine called a sequenator
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? in peptide bonding (chapter 4)
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angle around the ?-carbon - amide nitrogen bond
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? in peptide bonding (chapter 4)
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angle around the ?-carbon - carbonyl carbon bond
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Ramachandran Plot (4)
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shows favoreable ?-? angle combinations. 3 main "wells" for ?-helices, ?-sheets, and left handed ?-helices
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Levinthal's Paradox (4)
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protein folding cannot be a completely random, trial and error process
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chaperonins (4)
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elaborite protein complexes required for the folding of a number of cellular proteins that do not fold spontaneously
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Henderson-Hasselbach Equation (2)
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pH = pKa + log([A-]/[HA])
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which amino acids are not found in ?-helices? (4)
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glycine and proline. glycine is too flexible, proline is too rigid to rotate.
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which amino acids are commonly found in ? turns? (4)
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glycine, because it is small and flexible, and proline because it forms cis conformation in tight turns.
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?-mercaptoethanol (4)
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breaks disulfide bonds
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circular dichroism (4)
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technique that measures the amount of helical structures in macromolecule (protein is denatured)
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Acid Dissasociation constant Ka (2)
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quantitative measure of the strength of an acid in solution
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Size-exclusion chromatography (3)
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Separates proteins according to size. Large proteins emerge from the column before small ones (counterintuitive result). The solid phase consists of beads with engineered pores or cavities of a particular size. Large proteins cannot enter the cavities, and so take a short (and rapid) path through the column, around the beads. Small proteins enter the cavities, and migrate through the column more slowly as a result
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Affinity chromatography (3)
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based on the binding affinity of a protein. The beads in the column have a covalently attached chemical group. A protein with affinity for this particular chemical group will bind to the beads in the column, and its migration will be retarded as a result
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HPLC, or high-performance liquid chromatography.
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pumps speed the movement of the protein molecules down the column, as well as higher-quality chromatographic materials that can withstand the crushing force of the pressurized flow. By reducing the transit time on the column, HPLC can limit diffusional spreading of protein bands and thus greatly improve resolution.
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cation-exchange chromatography (3)
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solid matrix (stationary phase) has negatively charged groups. In the mobile phase, proteins with a net positive charge migrate through the matrix more slowly than those with a net negative charge. The two types of protein can separate into two distinct bands.
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Induced fit
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conformational changes (in either ligand or protein) that can occur upon ligand binding in order for tighter binding of ligand. ex: HbA
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porphin
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organic compound that is aromatic and heterocyclic, consisting of 4 pyrole rings joined by 4 methine (=CH-) groups to form a larger macrocycle ring. Ex: hemoglobin
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hemoglobin, HbA (5)
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sigmoidal curve (positive cooperativity); four subunits bind four O2; binding one O2 increases affinity for binding the other three (heme-heme interaction)
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ligand (5)
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any molecule that binds reversibly to a protein
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myoglobin, Mb (5)
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hyperbolic curve; one subunit binds one O2; higher affinity for oxygen than HbA, binds oxygen dropped by HbA in low oxygen environments (myo = muscle)
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Hill plot (5)
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turns sigmoid into straight lines. slope = n (# of binding sites). allows measurement of cooperative binding sites.
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Hill number, n/nH (chapter 5)
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provides a measure of the degree of cooperativity between states. nH 1.0, positive cooperativity, binding of first ligand makes binding of second MORE likely. nH = 1.0, not a cooperative system
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Hemoglobin "Tense-state"
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low pH, high CO2, high 2,3-BPG
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PO2 (5)
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about 13 kPa in lungs, 4 kPa in tissues
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Bohr effect (5)
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effect of H+ and CO2 on the binding and release of O2 from Hb. O2 binds well at higher pH and low CO2.
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2,3-bisphosphoglycerate (5)
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decreases affinity of Hb for O2, stabilizing T-state
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antibodies or immunoglobulins, Ig (chapter 5)
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bind bacteria, viruses, or large molecules identified as foreign and target them for destruction
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ELISA (enzyme-linked immunosorbent assay) (5)
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allows for rapid screening and quantification of the presence of an antigen in a sample.
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epitope (antigenic determinant) (5)
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where individual antibodies or t-receptors bind on antigen
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1) competitive inhibitors 2) uncompetitive inhibitors 3) mixed inhibitors (chapter 6)
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1) Km increases, no effect on Vmax, same y-intercept, increasing slope, increased substrate can overcome 2) Vmax decreases, y-intercepts increase, constant slope, increased substrate cannot overcome 3) Km increases, Vmax decreases, y-intercepts increase, slope increases, increased substrate cannot overcome
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?Gb - binding energy (6)
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major source of free energy used by enzymes to lower the activation energies of reactions
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michealis-menton equation (6)
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V0 = Vmax [S] / (Km + [S])
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Km in michaelis-menten (6)
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Km = [S] when V0 = 0.5(Vmax)
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Kcat (6)
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rate limiting step in any enzyme catalyzed reaction and saturation. Kcat = Vmax / Et
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chymotrypsin (6)
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cleaves proteins on C-terminal end of Phe, Trp, and Tyr
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mutarotation (7)
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conversion from ? to ? forms of sugar at the anomeric carbon
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ionophore (11)
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hydrophobic molecule that binds to ions and carries them through cell membranes disrupting concentration gradients.
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ethanol fermentation (14)
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pyruvate --> acetylaldehyde --> ethanol. uses pyruvate decarboxylase and alcohol dehydrogenase. NADH --> CO2 (TPP) + NAD+
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what enzyme is used in converting pyruvate to oxaloacetate? (14)
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pyruvate carboxylase (in mitochondria). cofactors include biotin (carries activated biocarbonate). ATP is used.
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pyruvate dehydrogenase complex enzymes (14)
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1) Pyruvate dehydrogenase, 2) dihydrolipoyl transacetylase, 3) dihydrolipoyl dehydrogenase
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stimulates gluconeogenesis / inhibits glycolysis (14)
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acetyl-CoA, glucagon
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stimulates glycolysis / stimulates glycolysis (14)
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ADP, AMP, insulin
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sum for gluconeogenesis (14)
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2 pyruvate + 4ATP + 2GTP + 2NADH + 2H+ + 4H2O --> glucose + 4ADP + 2GDP + 2NAD + 6Pi
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ultimate electron acceptor of oxidative decarboxylation in the TCA cycle
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O2
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Hexokinase IV (glucokinase)
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inhibited by fructose 6-phosphate and G6P. found in hepatocytes and ?cells of pancreas; buffers blood glucose
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PFK -1
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activated by AMP, F26BP.
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pyruvate kinase
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allosterically inhibited by high ATP; activated by F1,6-BPase
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pyruvate carboxylase
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activated by acetyl-CoA
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carnitine shuttle (17, p. 634)
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transports free fatty acids across inner mitochondrial membrane. 3 enzymatic reactions: 1) esterification to CoA (acyl CoA synthetases) 2) transesterification to carnitine (folllowed by transport) 3) transesterification back to CoA
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electron carriers for the electron transport chain (19)
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1) coenzyme Q - ubiquinone 2) cytochromes (heme prosthetic groups)
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plastocyanin (19)
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carries electrons from photosystem II to photosystem I
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amylose chain (20)
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?-1,4-linkages that produce a coiled helix similar to an ?-helix. has a reducing end and a non-reducing end
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anomeric carbon (20)
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carbon that is cyclized. always the same as the aldo or keto carbon in the linear form.
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mobilization of fatty acids
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stimulated by hormones glucagon and epinephrine
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promoter
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identifies the start of a gene, which strand is to be copied, and the direction in which to copy it.
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operator
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site of repressor binding
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