My protease has a globular structure with beta sheets, alpha helix and many shar
ID: 314612 • Letter: M
Question
My protease has a globular structure with beta sheets, alpha helix and many sharp turns. It has a pocket where it binds amino acids and it has a flexible hinge that is regulated to cover the pocket so the enzyme can be turned off. Match the amino acid to the MOST APPROPRIATE location in/on the enzyme.
open hinge closed hinge
proline
glycine
histidine
phenylalanine
serine
none of these
a sharp fixed turn in the protein backbone
a flexible hinge
the active site
internal within the enzyme
external on the enzyme
cysteineproline
-glycine
histidine
phenylalanine
serine
A.none of these
B.a sharp fixed turn in the protein backbone
C.a flexible hinge
D.the active site
E.internal within the enzyme
F.external on the enzyme
Explanation / Answer
cysteine - the active site
proline - a sharp fixed turn in the protein backbone
glycine - a flexible hinge
histidine - none of these
phenylalanine - internal within the enzyme
serine - external on the enzyme
histidine is used to activate cysteine and threonine on proteases so that it would function.
the built-in bend in proline and lack of large side chain in glycine allow the protein to fold into a tight U-shape.
since phenylaanine is hydrophobic, it is buried inside the globular protein.
serine is hydrophilic.
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