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Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Related Experiment Video

Updated: Apr 11, 2026

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Multivalent weak contacts shape chaperone-nascent protein interactions.

Nandakumar Rajasekaran¹, Dmitri Toptygin¹, Ting-Wei Liao²

¹Department of Biology, Johns Hopkins University.

Biorxiv : the Preprint Server for Biology

|April 10, 2026

Summary

This summary is machine-generated.

Trigger factor, a bacterial chaperone, uses multiple weak, dynamic interactions to bind nascent proteins on ribosomes. This multivalent binding stabilizes proteins during early folding stages.

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Area of Science:

Molecular biology
Biophysics
Protein folding

Background:

Molecular chaperones are essential for preventing protein misfolding within cells.
Trigger factor is a ribosome-associated chaperone that assists nascent polypeptide folding.
The precise mechanisms of trigger factor's dynamic interactions with emerging proteins are not fully understood.

Purpose of the Study:

To directly observe and characterize the interactions between trigger factor and ribosome-bound nascent proteins.
To elucidate the nature and dynamics of trigger factor binding as polypeptide chains elongate.

Main Methods:

Single-molecule fluorescence techniques.
Optical tweezers to apply mechanical force.
Direct observation of trigger factor binding to client proteins at various chain lengths.

Main Results:

Trigger factor binding is characterized by multiple weak, dynamic interactions.
These interactions are established after ribosome docking and evolve during polypeptide elongation.
Mechanical force disrupts trigger factor binding, supporting a multivalent interaction model.

Conclusions:

Trigger factor employs a multivalent binding strategy to interact with nascent proteins.
This dynamic binding mode likely stabilizes proteins against misfolding while allowing conformational exploration.
Understanding these interactions provides insights into cotranslational protein folding.