Question

Chaperone proteins can aid in protein folding by doing which of the following?

1) Steering partially folded polypeptide chains along the most energetically favorable folding pathway
2) Isolating a polypeptide chain within the crowded cytoplasm to prevent aggregation of proteins
3) Providing the binding energy for possible protein conformations before achieving the one that is most stable

Answer 1

Chaperone proteins aid in protein folding by steering folding pathways, isolating polypeptide chains to prevent aggregation, and providing binding energy for stable conformations, ensuring correct protein function.

Step-by-step explanation:

Chaperone proteins assist in the process of protein folding by:

1. Steering partially folded polypeptide chains along the most energetically favorable folding pathway.
2. Isolating a polypeptide chain within the crowded cytoplasm to prevent aggregation of proteins.
3. Providing the binding energy for possible protein conformations before achieving the one that is most stable.

These actions help ensure that the proteins fold correctly, which is crucial for their functionality. Chaperone proteins such as HSP70 (heat-shock 70 protein) play a key role in aiding the folding and unfolding of proteins during their transport into cellular compartments like mitochondria, preventing protein dysfunction caused by incorrect folding in abnormal temperature or pH conditions.