My protease has a globular structure with beta sheets, alpha helix and many shar
ID: 186905 • 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 A. cysteine proline glycine histidine phenylalanine serine none of these B. a sharp fixed turn in the protein backbone C a flexible hinge D the active site internal within the enzyme F. external on the enzymeExplanation / Answer
Flexible hinge. : Proline C
Sharp fixed turn in protein backbone: glycine B
Active site : serine D
None of these : phenylalanine A
Internal within the enzyme : cysteine E
External on the enzyme : histidine F
Proline could act as a flexible hinge. It bind helices by an angle at 10-20 A. Proline has one fixed dihydral angle, for this reason segment containing proline has more rigidity and provide locus for protein folding and assembly. Proline could act as flexible element that nediate rigid body motion of helical segment.
Glycin often found in loop region where the polypeptide chain needs to make sharp turn because it is less strically hindered as compared to other amino acid because has no side chain.
Serine found in active site of enzyme which responsible for its enzymatic action.
Protease is globular protein which is soluble in aqueous media so hydrophilic amino acid present outside and hydrophobic amino acid present inside. Histidine is hydrophilic located on external site whereas hydrophobic cysteine located within the enzyme.
Related Questions
Navigate
Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.