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Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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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: Mar 10, 2026

Interview: Protein Folding and Studies of Neurodegenerative Diseases

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Published on: July 16, 2008

A driving force for polypeptide and protein collapse.

Antonello Merlino¹, Nicola Pontillo¹, Giuseppe Graziano²

¹Dipartimento di Scienze Chimiche, Università degli Studi di Napoli Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia, 80126 Napoli, Italy.

Physical Chemistry Chemical Physics : PCCP

|December 9, 2016

Summary

Polypeptide chains collapse in water due to a redefined hydrophobic effect, driven by increased water entropy, not just nonpolar side chains. This challenges traditional protein folding theories.

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Area of Science:

Biophysics
Computational Chemistry
Biochemistry

Background:

Experimental and computational studies show polyglycine chains (15-25 residues) collapse in water at room temperature.
This observation contradicts the established theory that the hydrophobic effect, driven by nonpolar side chain burial, is the primary force for polypeptide collapse and folding.

Purpose of the Study:

To propose a redefined hydrophobic effect as the driving force for polyglycine collapse.
To demonstrate that chain collapse is characterized by a gain in water molecule translational entropy.

Main Methods:

Utilized experimental measurements.
Employed computational results.

Main Results:

Polypeptide chains of 15-25 glycine residues were observed to collapse into compact structures in water.
The study suggests the hydrophobic effect should be redefined by the decrease in solvent-excluded volume during collapse, leading to increased translational entropy of water molecules.

Conclusions:

The hydrophobic effect, redefined by solvent-excluded volume and water entropy, drives polypeptide collapse.
Nonpolar side chains may be less critical for collapse than previously thought, though important for unique structure formation.