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BCH 4053 exam 3 Questions & Verified Answers, 2025 / 2026., Exams of Nursing

BCH 4053 exam 3 Questions & Verified Answers, 2025 / 2026.

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2024/2025

Available from 07/15/2025

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BCH 4053 exam 3 Questions & Verified
Answers, 2025 / 2026.
allosteric regulation by covalent modification - CORRECT ANSWERS phosphorylation of Serine,
Threonine, and Tyrosine, mediated by kinases and phosphatases
glycogen phosphorylase (GPase) - CORRECT ANSWERS breaks down glycogen
expressed in muscle
phosphorylated at Ser 14
when GPase is phosphorylated - CORRECT ANSWERS phosphorylase a
GPase is dephosphorylated - CORRECT ANSWERS phosphorylase b
GPase structure and function - CORRECT ANSWERS dimer with two conformations (R/T)
shift to the R state - CORRECT ANSWERS phosphorylation
adding complexity to regulation by phosphorylation - CORRECT ANSWERS a - inhibited by
glucose
b- activated by AMP, inhibited by ATP or G6P
going from the T state to the R state
drug discovery - CORRECT ANSWERS starts with a lead compound; natural product like a plant;
should have high affinity for target
pf3
pf4
pf5

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BCH 4053 exam 3 Questions & Verified

Answers, 2025 / 2026.

allosteric regulation by covalent modification - CORRECT ANSWERS phosphorylation of Serine, Threonine, and Tyrosine, mediated by kinases and phosphatases

glycogen phosphorylase (GPase) - CORRECT ANSWERS breaks down glycogen

expressed in muscle

phosphorylated at Ser 14

when GPase is phosphorylated - CORRECT ANSWERS phosphorylase a

GPase is dephosphorylated - CORRECT ANSWERS phosphorylase b

GPase structure and function - CORRECT ANSWERS dimer with two conformations (R/T)

shift to the R state - CORRECT ANSWERS phosphorylation

adding complexity to regulation by phosphorylation - CORRECT ANSWERS a - inhibited by glucose

b- activated by AMP, inhibited by ATP or G6P

going from the T state to the R state

drug discovery - CORRECT ANSWERS starts with a lead compound; natural product like a plant; should have high affinity for target

lead compounds - CORRECT ANSWERS fine tune drugs

  • promote tighter binding
  • minimize side effects
  • modifications - methyl, chloryl, hydroxyl

bioavailability - CORRECT ANSWERS how much drug reaches target; must be easy to administer

roles of hormones (3) - CORRECT ANSWERS maintain homeostasis

released in response to stimuli

regulate cyclical processes

receptors - CORRECT ANSWERS generate second messengers or activate kinase/phosphatase which activate an enzyme cascade

epinephrine and norepinephrine - CORRECT ANSWERS fight or flight response

steroid hormones - CORRECT ANSWERS secreted by gonads and adrenal glands

glucorticoids - CORRECT ANSWERS stimulates glycogen and fat breakdown

mineralcorticoids - CORRECT ANSWERS regulate excretion salt and water by kidneys

water insoluble hormones - CORRECT ANSWERS transported by transcortin; bound intracellularly and spontaneously pass through membrane

growth hormone - CORRECT ANSWERS secreted by pituitary gland; peptide hormones; stimulate growth; binds extracellularly by GH receptor

SH2 domains - CORRECT ANSWERS all sorts of proteins: kinases, phosphatases, G proteins

Some proteins have both SH2 and SH3 - CORRECT ANSWERS SH2 at one end and SH3 at other end

SH3 domains - CORRECT ANSWERS bind proline rich regions, mediate protein/protein interactions

RTK activation - CORRECT ANSWERS sometimes result in activation of G protein

Example of G protein - CORRECT ANSWERS Ras activation by growth factor

Ras- like proteins - CORRECT ANSWERS guanine exchange (GEF) and GTPase activating proteins(GAP)

types of catalytic mechanisms - CORRECT ANSWERS acid base

covalent

metal ion

proximity and orientation effects

preferential binding of transition state

enzyme properties - CORRECT ANSWERS differ in reacton rate, reaction conditions, reaction speficity, and control

active site limits an enzyme's activity to specific substrates

higher rates of reaction, mild conditions

specific - CORRECT ANSWERS H+ or OH transferred

general - CORRECT ANSWERS H+ or OH generated from TS; rate limiting

histidine - CORRECT ANSWERS side chain is 7 so it is a base and acid

geometric complementary - CORRECT ANSWERS substrate binding site on enzyme is complementary to shape of substrate

enzymes are stereospecific - CORRECT ANSWERS highly stereocspecific in chiral substrates and and catalysis- because of chirality of amino acids in enzyme

cofactors - CORRECT ANSWERS chemical teeth for enzymes; can be metal ions

coenzymes - CORRECT ANSWERS organic molecules that are cofactors

NAD+ and NADP+ - CORRECT ANSWERS examples of cosubstrates

an enzyme provides - CORRECT ANSWERS lower energy pathway from substrate to product - does not affect the overall free energy change

reaction coordinate - CORRECT ANSWERS when reactants approach each other along the minimum free energy path

delta G crit - CORRECT ANSWERS free energy of actication - difference between beginning reactants and transition state

second stage - CORRECT ANSWERS withdrawal of e- from rxn center by electrphile

3rd stage of CC - CORRECT ANSWERS elimination of catalyst

metal ions - CORRECT ANSWERS orient substrates for reaction

oxidation-reduction rxns using oxidation state

shield negative charges

carbonic anhydrase - CORRECT ANSWERS has Zn2+ and polarizes h2O so it does not form OH and reacts with CO

proximity and orientation - CORRECT ANSWERS electrostatic catalysis, reduce rotation, right orientation, and bring substa

three key residues for catalysis - catalytic triad - CORRECT ANSWERS asp- 102 orients and polarizes his 57

his -57 - base and acid

ser- 195 - covalent bond with peptide

oxyanion hole - CORRECT ANSWERS tetrahedral intermediate at high energy state; makes hydrogen bonds with enzyme, binding of transition state

low barrier hydrogen bonds - CORRECT ANSWERS short and strong, chymotrysin transitionstate stabilizer