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BCH 369 TESTED QUESTIONS WITH VERIFIED ANSWERS

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BCH 369 TESTED QUESTIONS WITH VERIFIED ANSWERS What is the role of the disulfide bond is oxytocin and vasopresin? - Answer-the disulfide bond is responsible for the cyclic structure of both Match protein structure: 1. The order of amino acid residues in the polypeptide chain 2. The interaction between subunits in proteins that consist of more than one polypeptide chain 3. The hydrogen-bonded arrangment of the polypeptide backbone 4. The 3-D arrangement of all atoms - Answer-1. Primary 2. Quaternary 3. Secondary 4. Tertiary Define denaturation in terms of the effects of secondary, terry and quaternary structure - Answer-When a protein is denatured, the interactions that determine secondary, tertiary and any quaternary structures are overcome by the presence of the denaturing agent. Only the primary structure remains intact. What is the nature of "random" structure in proteins? - Answer-The random portions of a protein do not contain structural motifs that are repeated within the protein, such as alpha-helix or Beta-pleaded sheet, but 3D features of these parts of the protein are repeated from one molecule to another. Thus, the term random is somewhat of a misnomer. Rationalize: 1. Serine is the amino acid residue that can be replaced with the least effect on protein structure and function 2. Replacement of tryptophan cases the greatest effect on protein structure and function 3. Replacements such as Lys - Arg and Lys -Ile usually have very little effect on protein structure and function - Answer-1. Serine has a small side chain that can fit in any relatively polar envirionment 2. Tryptophan has the largest side chain of any of the common amino acids, and it tends to require a non polar environment 3. Lysine and arginine are both basic amino acids; exchanging one for the other would not affect the side-chain pKa in a significant way. Similar reasoning applies to Lys and Leu

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BCH 369 CHAPTER 7 TEST QUESTIONS
WITH ANSWERS ALL REVISED AND
UPDATED
random mechanism - Answer-A multisubunit reaction without a compulsory order of
substrate binding to the enzyme.

ordered mechanism - Answer-A multisubunit reaction with a compulsory order of
substrate binding to the enzyme.

Ping pong mechanism - Answer-An enzymatic reaction in which one or more products
are released before all the substrates have bound to the enzyme.

allosteric enzyme - Answer-1

cooperativity - Answer-2

rational drug design - Answer-The synthesis of more effective drugs based on detailed
knowledge of the target molecule's structure and function.

pharmacokinetics - Answer-The behavior of a drug in the body, including its metabolism
and excretion.

clinical trial - Answer-A three-phase series of tests of a drug's safety and effectiveness
in human subjects.

Irreversible inhibitor - Answer-A molecule that binds to and permanently inactivates an
enzyme.

suicide substrate - Answer-A molecule that chemically inactivates an enzyme only after
undergoing part of the normal catalyric reaction.

competitive inhibition - Answer-A form of enzyme inhibition in which a substance
competes with the substrate for binding to the enzyme active site and thereby appears
to increase Km.

inhibition constant (KI) - Answer-The dissociation constant for the complex between an
enzyme and a reversible inhibitor.

EI complex - Answer-The noncovalent complex that forms between an enzyme and a
reversible inhibitor.

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