A type Il beta turn has what residue as one of the four residues that make up the turn? OAP O B. G O D.A O E. Q Once a substrate is bound to the active site, there are a varety of mechanisms that aid in the cdeavage and formation of benas. These incue. OA General acid base catalysis by amino acid side chains which can act as proton donors and acceptors. OB. Metal ion catalysis where tightly bound metal ligands can participate in catalus. Oc covalent catalysis where the enzyme forms transient covalent bonds with reactants and these bonds are later broken OD. all of the above E only A and C The Ramachandran plot describes the peptide conformation by illustrating the position of the dihedral angles that can rotate following. OA side-chain steric hindrance • B. restrictions imposed by secondary structure C. main-chain clashes from the bulky carbonyl oxygen or amide nitrogen with other main-chain atoms or side-chains D. All of the above E. None of the above

A type Il beta turn has what residue as one of the four residues that make up the turn? OAP O B. G O D.A O E. Q Once a substrate is bound to the active site, there are a varety of mechanisms that aid in the cdeavage and formation of benas. These incue. OA General acid base catalysis by amino acid side chains which can act as proton donors and acceptors. OB. Metal ion catalysis where tightly bound metal ligands can participate in catalus. Oc covalent catalysis where the enzyme forms transient covalent bonds with reactants and these bonds are later broken OD. all of the above E only A and C The Ramachandran plot describes the peptide conformation by illustrating the position of the dihedral angles that can rotate following. OA side-chain steric hindrance • B. restrictions imposed by secondary structure C. main-chain clashes from the bulky carbonyl oxygen or amide nitrogen with other main-chain atoms or side-chains D. All of the above E. None of the above

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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One of the reasons for oxidizing the disulfide bonds in RNase A before removing the urea in the Anfinsen experiment was to demonstrate that ... Urea promotes disulfide bond exchange O Incorrectly-folded proteins lose their enzymatic activity. Urea prevents disulfide bond formation. Urea forms thio-esters with reduced cysteines at pH 8.2 Disulfide bonds are required for enzyme activity.
A1
о 6. What is the catalytic triad and what particular protein family would you find this? What is the general role of the catalytic triad? Predict what would happen if Asp were mutated to Gly. ructure formation of alpha heli
7. An enzyme-catalyzed reaction proceeds by the mechanism below: E+S1ES --2E+P E+A 3 EA EA+S4→ EAS --5→ EA + P E+I6 → EI EAS +17→ EAIS -8 EIS + P A. B. C. E = enzyme, S = substrate, I = inhibitor, P = product and A = activator Rate constants (k's) for the forward reactions are: K1, K2, k3, K4, k5, k6, k7, and k8 Rate constants (k's) for the reverse reactions are: k-1, k-3, K.4, k.6, and k.7 Write the enzyme balance for this mechanism. How many total equations will result from applying the RAPID EQUILIBRIUM ASSUMPTION? Using any concentrations of species in the mechanism and any of the rate constants (k's), write ONE of the equations that would result from applying the QUASI STEADY STATE ASSUMPTION. (ONLY ONE EQUATION; ANY OF THEM ARE FINE)
Which of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pH
Multifunctional protein kinases O phosphorylate various targets with the correct consensus sequence carry out phosphorylation as well as sulfonation reactions O remove phosphates through hydrolysis O have a very specific target that they phosphorylate conserve energy in the form of ATP from the degradation of proteins
4. The figure below shows ATP in the binding site of pyruvate kinase, an important enzyme in cellular respiration. Note that only amino acids involved in interactions in the binding site are shown. Lys His ATP NH ; afafafor OH OH qat Glu Tyr Asp a. What is the most likely chemical interaction occurring between the tyrosine and the ribose of ATP? b. List one mutation to the lysine (Lys) in the binding site that would likely result in the kinase NOT being able to bind ATP (state the change in amino acid, not in the DNA or mRNA). In one sentence, explain why this mutation would likely lead to this change. Be as specific as possible.
A plot of 1½5 venut VSL, Glld a Br-weaver Burk or double-reciprocal plot, is a useful tool for identifying the type of Madily each gaph by dragging the endpoints to show the various types of enzyme inhibition. What is the inhibition mechanism for the competitive inhibitor? The inhibisr binde cenly in recemyne The inhibitor bindx only lo cozyme- substrate complexe The inhibike binds tas bath free enzyme and enzyme xubxirale completes with identical binding axolante. The inhibikr binds to both free enzyme and cozyme substrate completes with different binding constants. What is the inhibition mechaniam for the uncompetitive inhibitor? The inhibitor binds only to free ENZYMES. The inhibitor bind is both tree enzyme and enzyme auhdraic compleaca with identical binding coulants. The inhibar binds only in enzyme ubrale complex.ca. The inhibir bindis in bath free enzyme and cxyme aubairale complicaca with dill crcnt binding costanix. LAST Nompumps dve shk with inbibus WHEY Pullie mechanism kot…
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Concerning enzymatic activity, a larger Km value indicates a/an: Select one: O lower affinity for its substrate O inhibitory process O larger enzyme O larger Vmax O greater affinity for the substrate Which is the least common type of chemical bond? Select one: O Hydrogen O Peptide O Covalent O lonic O Disulphide D-gluconic acid is: Select one: O an integral membrane protein O a codon O an oxidized sugar O phosphorylated O a large lipid molecule
Which one of the following best explains the distinctive effect of an uncompetitive inhibitor on Km, according to our coverage? If S binds first, I may never bind and P can be formed. When ESI complexes form, S is trapped and it is as though there is a lower concentration of E.
Changing which pairs of the amino acids is most likely to directly lead to the most severe problems with substrate (Blue) binding by the protein depicted by the red ribbon.