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BCH210 EXAM QUESTIONS WITH COMPLETE SOLUTIONS

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BCH210 EXAM QUESTIONS WITH COMPLETE SOLUTIONS structure of glucose transporter - Answer-many trans helices, packed into bundles, 12 segments all together - 2 conformational states; inward facing and outward facing insulin receptor structure - Answer-2 subunits made up of alpha and beta chai...

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  • August 30, 2024
  • 8
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers

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  • bch210
  • bch210 exam questions with complete solutions
  • structure of glucose transporter

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BCH210 EXAM QUESTIONS WITH
COMPLETE SOLUTIONS
structure of glucose transporter - Answer-many trans helices, packed into bundles, 12
segments all together
- 2 conformational states; inward facing and outward facing

insulin receptor structure - Answer-2 subunits made up of alpha and beta chains joined
by disulfide bonds

what stabilizes ribonuclease? - Answer-disulfide bonds

urea - Answer-disrupts non covalent bonds

b-mercaptoethanol - Answer-breaks disulfide bonds

4 approaches to genetic engineering - Answer-clone the gene of interest, insert gene
into a replication vector, insert the plasmid into a bacterial host, grow the bacteria

4 components of plasmids - Answer--origin of replication, selectable marker, multiple
cloning sites, promoter

endonucleases - Answer-cleave DNA at palindromic sites

polymerases - Answer-extend DNA chains by forming phosphoester bonds

ligases - Answer-join two phosphoester bonds together

SDS - Answer-denaturing detegent, dissolves membranes and solubilizes proteins

polyacrylamide gel - Answer-gel matrix to separate proteins

3 amino acids involved in serine protease active site - Answer-ser, his, asp

steps of subtilisin catalytic triad - Answer-1) transition state is stabilized, peptide bond
cleavage occur, substrate covalently binds to enzymes Ser221, second transition state
occurs, enzyme active site is recovered

protease - Answer-enzymes that catalyze breaking of peptide bonds

subtilisin - Answer-protease that initiates nucleophilic attack on peptide bonds through a
serine residue at an active site

, when they tried to engineer disulphide bonds into subtilisin; what aa switch did they
make? - Answer-Serine to Cysteine

how many consecutive helical aa before its classified as Alpha Helix - Answer-4

how many consecutive b sheet aa before its called a Beta Sheet - Answer-min 3

how many consecutive position of b-turns before its called b-turn - Answer-4

top alpha helix forming residues - Answer-Glu, Met, ala, leu, lys

poor alpha helix residues - Answer-gly, pro

top beta sheet forming residues - Answer-val, ile, tyr

poor beta sheet forming aa - Answer-glu, asp, pro

top b-turn - Answer-asn, pro, gly, asp, ser

poor b-turn aa - Answer-ile, val, leu, phe, met

best beta turn - Answer-asn-pro-gly-gly

fusion protein - Answer-found in expression vectors, aid in solubilization of expressed
protein

components of fusion protein - Answer-thioredoxin, his tag, wb tag, desired protein

glucagon structure - Answer-n terminal is beta strand, c terminal is alpha helix

glucagon at high concentration forms what structure (likely what location) - Answer-beta
sheet (pancreas)

glucagon at low concentration forms what structure (likely what location) - Answer-alpha
helix (blood)

what form is glucagon when bound to receptor - Answer-alpha helix

types of protein chromatography - Answer-gel filtration, ion exchange, hplc, affinity
chromatography

gel filtration - Answer-separates proteins based on size

ion exchange - Answer-separates proteins based on net charge

hplc - Answer-separates proteins based on hydrophobicity

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