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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

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.
The...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

Amyloid Fibrils

Amyloid Fibrils

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Related Experiment Video

Updated: Mar 9, 2026

Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.

H Jane Dyson¹, Peter E Wright¹

¹Department of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla California 92037, United States.

Accounts of Chemical Research

|December 30, 2016

Summary

The amino acid sequence dictates protein folding pathways and structures. Researchers used advanced techniques to map apomyoglobin folding, revealing key intermediates and residue-specific dynamics.

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Area of Science:

Biophysics
Protein folding dynamics
Structural biology

Background:

Protein folding is governed by biophysical principles, with the amino acid sequence determining the final structure and folding pathway.
Understanding protein folding mechanisms is crucial for deciphering biological functions and diseases.

Purpose of the Study:

To elucidate the underlying principles of protein folding by focusing on the globin family, specifically apomyoglobin.
To characterize the equilibrium and kinetic intermediates of apomyoglobin folding structurally and dynamically.
To delineate the complete folding pathway at a residue-specific level.

Main Methods:

Utilized rapid-mixing techniques (stopped-flow, quench-flow) with circular dichroism (CD), fluorescence spectroscopy, and mass spectrometry.
Employed nuclear magnetic resonance (NMR) spectroscopy, including residual dipolar couplings and relaxation dispersion measurements.
Characterized equilibrium intermediates at pH ~4 and unfolded state ensembles using solution methods.

Main Results:

Apomyoglobin (apoMb) folds in approximately 2 seconds via rapidly forming obligatory intermediates.
Identified and structurally characterized equilibrium and kinetic intermediates, providing insights into the folding pathway.
Advanced NMR techniques revealed residue-specific dynamics and probed low-concentration invisible states.

Conclusions:

The amino acid sequence is the ultimate determinant of protein folding initiation and progression towards the native state.
Detailed characterization of apomyoglobin folding provides a model system for understanding general protein folding principles.
The study offers a comprehensive view of apomyoglobin folding, linking sequence to structure and dynamics.