BCH210 EXAM QUESTIONS WITH ALL ANSWERS REVISED AND VERIFIED
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Course
BCH210
Institution
BCH210
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...
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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