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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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Related Experiment Video

Updated: Feb 28, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

The case for defined protein folding pathways.

S Walter Englander¹, Leland Mayne²

¹The Johnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104 engl@mail.med.upenn.edu.

Proceedings of the National Academy of Sciences of the United States of America

|June 21, 2017

Summary

This summary is machine-generated.

Proteins fold via many pathways, but these microscopic trajectories lack the bias for native interactions. A defined-pathway model, using foldons, explains reproducible protein folding and native structure selection.

Keywords:

energy landscape theory foldons protein folding

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Last Updated: Feb 28, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

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Assays for the Degradation of Misfolded Proteins in Cells

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Microfluidic Mixers for Studying Protein Folding

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Published on: April 10, 2012

Area of Science:

Biophysics
Molecular Biology
Protein Dynamics

Background:

The energy landscape model posits proteins fold via numerous heterogeneous pathways.
Experimental evidence suggests proteins fold through defined pathways involving cooperative units called foldons.

Purpose of the Study:

To compare the many-pathway protein folding model with the defined-pathway model.
To analyze the functional significance of microscopic folding trajectories.

Main Methods:

Theoretical analysis of energy landscape considerations.
Experimental characterization of protein folding pathways.
Analysis of foldon cooperative units in protein assembly.

Main Results:

Many microscopic folding trajectories lack significant distinction and the necessary bias for native interactions.
Proteins fold in a reproducible, stepwise manner, one foldon unit at a time.
Foldon interactions encode both native structure and folding pathways.

Conclusions:

The defined-pathway model, based on foldons, provides a more accurate explanation for efficient protein folding and native structure selection.
Quantized native structure and stepwise folding likely coevolved in ancient proteins.