What will be the effect on protein function if each polypeptide adopted only a single, inflexible shape based on its primary structure?

A) The protein ability to catalyze would be impaired. The tertiary structure could not appear, so those proteins could not perform their function.

B) The ability to regulate protein activity would be impaired. The peptide bonds would not be so stable compared to linkages in other types of macromolecules, so those proteins could not perform their function.

C) The ability to regulate protein activity would be impaired. The proteins would be either permanently active or inactive, depending on how they are folded.

D) The proteins would perform their functions normally.

Question

27-08-2021
Biology

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What will be the effect on protein function if each polypeptide adopted only a single, inflexible shape based on its primary structure?

A) The protein ability to catalyze would be impaired. The tertiary structure could not appear, so those proteins could not perform their function.

B) The ability to regulate protein activity would be impaired. The peptide bonds would not be so stable compared to linkages in other types of macromolecules, so those proteins could not perform their function.

C) The ability to regulate protein activity would be impaired. The proteins would be either permanently active or inactive, depending on how they are folded.

D) The proteins would perform their functions normally.

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luisvaschetto luisvaschetto · Answer 1 · 2021-08-30T16:09:02+02:00

The ability to regulate protein activity would be impaired. The proteins would be either permanently active or inactive, depending on how they are folded (Option C).

Proteins are complex biomolecules composed of linear chains of amino acids that interact to produce a final three-dimensional (3D) protein structure.

Protein folding refers to the cellular mechanism by which proteins are folded to render a biologically active protein.

Different heat shock proteins (Hsp) are involved in protein folding.

If a protein or its subunits are not correctly folded, then it remains inactive because there is no interaction with its corresponding molecular partners (e.g., another protein in protein-protein interactions or DNA in the case of a transcription factor).

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