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

See similar textbooks

Similar questions

The role of Zn2+ in catalysis is usually to: a. Stabilize a (-) charge in the transition state O b. Act as a nucleophile Oc. Act as a base Od. Destabilize a (-) charge in the transition state
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A
The key catalytic amino acids of the lysozyme active site in the free enzyme are Glu 35 with a protonated side chain and Asp 52 with a deprotonated side chain. From this observation, lysozyme requires for effective catalysis. O A. an Asp in a nonpolar environment O B. a Glu that functions as an acid catalyst O C.a Glu functions as a covalent catalyst O D. All of the above
The amino acid histidine has been found to participate in both acid and base catalysis in many enzymatic reactions. Which of the following describes histidine? A. Its R group acts as proton donor at pH 7.0 B. Its R group acts as electron pair acceptor at pH 7.0 C. Its R group acts as proton acceptor at pH 7.0 D. Its R group helps in the proteolytic activity by acting as both proton donor and proton acceptor at pH 7.0
Which of the following is false regarding Serine Proteases? O They employ general acid-base catalysis They contain a catalytic Triad of His, Ser, and Asp residues They employ metal ion catalysis O They cleave simple organic ester bonds near larger residues
What are the effects of different light colors in photosynthesis? Different light colors will change the rate of photosynthesis Light color does not affect photosynthesis Carbohydrates are metabolized by light Photosynthesis does not require light
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase A-ase Acetate Deacetylase D Protease B-ase C-ase A-ase ABC- What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. F 1 M The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. 1 O Match the specificity pocket (identified by red number) to the residue that occupies it. 3 R Match the specificity pocket (identified by red number) to the residue that occupies it. 4 W 2 1. D 2. E 3. F 4. R 5. W 6. Y
Consider the following diagram of an enzyme capa- ble of interacting with two different substrates, Z and S: Eo ka k on off 'off Es Ez Derive expressions for the rates at which Z and S are transformed by the enzyme.
Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acetyl A-ase Acetate A-ase Deacetylase A-ase B-ase ABC- Isoenzymes Protease Inhibition What is the mechanism of regulation of A-ase? Reversible Covalent modification Isoenzymes What is the mechanism of regulation of A-ase? C-ase Reversible Covalent modification Proteolytic Activation Feedback Inhibition Positive allostery
Random Enzyme B requires Zn2+ (Zinc ion) to be functional. Zn2+ is a Cofactor Product Coenzyme Substrate Which of the following molecules would
Which of the following statements about ribozyme catalytic residues is INCORRECT? General acid catalysis requires the standarde nucleotide exchangeable proton acidities (represented by pKa values). Ribozymes work by lowering the AG‡ through transition state stabilization without changing the overall AG of the reaction. Some ribozymes cleave phosphodiester bonds, and like proteases, can be autocatalytic. There are fewer known classes of mammalian ribozymes than mammalian enzyles.