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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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

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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Molecular Chaperones and Protein Folding

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Related Experiment Video

Updated: Mar 29, 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

Evolution of a protein folding nucleus.

Xue Xia¹, Liam M Longo^1,2, Mason A Sutherland¹

¹Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida, 32306-4300.

Protein Science : a Publication of the Protein Society

|November 27, 2015

Summary

The folding nucleus (FN) is key to protein folding and evolution. Its structure changes during gene fusion and circular permutation, revealing insights into protein architecture evolution and cyclic symmetry.

Keywords:

folding pathway folding transition state phi-value protein design protein symmetry β-trefoil

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Last Updated: Mar 29, 2026

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

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Microfluidic Mixers for Studying Protein Folding

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Area of Science:

Protein biochemistry
Structural biology
Evolutionary biology

Background:

The folding nucleus (FN) is a cryptic element in protein primary structure essential for efficient folding pathways.
The FN is hypothesized as a heritable element in protein architecture evolution, but its structural changes remain poorly understood.

Purpose of the Study:

To characterize the folding nucleus (FN) in a designed symmetric β-trefoil protein.
To investigate structural changes in the FN during protein evolution, specifically through gene fusion and circular permutation.

Main Methods:

ϕ-value analysis was employed to characterize the FN.
Comparison of structure and folding properties of key foldable intermediates along an evolutionary trajectory.

Main Results:

The folding nucleus (FN) structurally acquired novel turn structures during gene fusion events.
Circular permutation adjusted the FN in response to destabilizing mutations, demonstrating FN plasticity.
The β-trefoil's C3 cyclic symmetry enabled FN plasticity via circular permutation.

Conclusions:

Gene fusion and circular permutation are mechanisms that structurally modify the folding nucleus (FN).
The plasticity of the FN, facilitated by intrinsic protein symmetry, offers a selective advantage.
This plasticity may explain the prevalence of cyclic structural symmetry in the proteome.