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BCH210 EXAM QUESTIONS WITH ALL ANSWERS REVISED AND VERIFIED

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BCH210 EXAM QUESTIONS WITH ALL ANSWERS REVISED AND VERIFIED what can beta sheets do for a protein. - Answer-bring distant parts of the protein together. what do the extended dimensions of a beta sheet allow it to do - Answer-partake in more interactions how many residues in a beta turn - An...

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  • August 30, 2024
  • 9
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers

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  • bch210
  • bch210 exam questions with all answers
  • what can beta sheets do for a protein

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BCH210 EXAM QUESTIONS WITH
ALL ANSWERS REVISED AND
VERIFIED
what can beta sheets do for a protein. - Answer-bring distant parts of the protein
together.

what do the extended dimensions of a beta sheet allow it to do - Answer-partake in
more interactions

how many residues in a beta turn - Answer-4

two places beta turns can be found - Answer-on the surface of globular proteins
connecting secondary structures

where do the hydrogen bonds form in a beta turn - Answer-between the carbonyl oxygrn
and amine nitrogen

is proline common in beta turns and where - Answer-yes in position 2

what other amino acids are common in beta turns - Answer-glycine, asparagine, serine

what do secondary structures come together to form - Answer-stable 3D structures
called motifs or larger domains

what can larger domains by connected by - Answer-flexible linker segments

what can ligands help to bind together - Answer-distinct regions of tertiary structures

which structures can disulfide bonds stabilize - Answer-tertiary and quaternary

may a domain function independantly to the rest of the protein - Answer-yes

where can zinc fingers be found - Answer-DNA binding proteins

what do zinc fingers contain - Answer-zinc ions that coordinate distnt side chains.
stabilizing domains.

quaternary structure - Answer-proteins with multiple identical or different subunits, held
together covalently or non-covalently

, give an example of a quaternary structure with identical subunits - Answer-alcohol
dehydrogenase

example of quaternary structure with different subunits - Answer-hemoglobin

are quaternary structures from different genes - Answer-they can be, or they can be
from the same one but are cleaved by post translational stuff.

which amount of subunit quaternary structures seem to prevail in nature - Answer-2 and
4

name ways that a protein can fold - Answer-- secondary structures form due to
favourable H bonding
- non-covalent interactions and disulfide bonds help to bring distant regions of. protein
together
- random coils may not be random they may be stable structures
- hydrophobic effect causes folding
- chaperones transiently bind to hydrophobic regions,
to prevent aggregations and allow proper folding.

rank the interactions - Answer-covalent>ionic=hydrogen=hydrophobic>VDW

essential ions vs coenzymes - Answer-essential ions help with enzymmatic activity
whereas coenzymes carry chemical groups of electrons.

strength of ionic interaction depends on - Answer-polarity of the charged species

another names for an electrostatic interaction - Answer-ionic bond, salt bridge

strength of hydrogen bond depends on - Answer-polarity of H bond donor and acceptor

strength of hydrophobic interactions depends on - Answer-the entropy of water being
released.

strength of VDW depends on - Answer-the size of the atoms as well as the distance
between them

what does the strength of the interaction usually correlate with in terms of the distance
between the molecules - Answer-the stronger the interaction, the closer together the
molecules.

which atom in a hydrogen bond acts as the acceptor - Answer-the electronegative one

do hydrogen bnds only occur within a molecule - Answer-no, they can form between
molecules aswell.

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