What is the effect of GroES binding to GroEL on the chamber structure?
Understand the Problem
The question is asking about the structural effects of GroES binding to GroEL on the chamber structure, specifically how it impacts the size and environment of the chamber in relation to protein folding.
Answer
GroES binding to GroEL enlarges the chamber for protein folding.
The binding of GroES to GroEL triggers a major conformational change in the cis ring, enlarging the chamber for the release and folding of the bound nonnative polypeptide.
Answer for screen readers
The binding of GroES to GroEL triggers a major conformational change in the cis ring, enlarging the chamber for the release and folding of the bound nonnative polypeptide.
More Information
The GroEL-GroES complex plays a crucial role in protein folding, ensuring proteins achieve the correct conformation crucial for their function. This system assists proteins in folding efficiently in a controlled environment.
Tips
A common mistake is assuming GroES binding does not change the chamber size. Remember, GroES causes a conformational change that results in an enlarged chamber.
Sources
- Effect of GroES binding to GroEL - sciencedirect.com
- The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding - cell.com
AI-generated content may contain errors. Please verify critical information
