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Related Concept Videos

Protein Folding01:25

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 Folding01:22

Protein Folding

Overview
Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

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 Folding03:00

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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: Jun 11, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

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

Published on: February 12, 2019

Proteins that switch folds.

Philip N Bryan1, John Orban

  • 1Institute for Bioscience and Biotechnology Research, Department of Bioengineering, University of Maryland, 9600 Gudelsky Drive, Rockville, MD 20850, USA. bryan@umbi.umd.edu

Current Opinion in Structural Biology
|July 2, 2010
PubMed
Summary
This summary is machine-generated.

Proteins can switch between different structures, revealing new functions. This protein fold switching highlights that a single amino acid sequence contains more information than previously understood.

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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

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Microfluidic Mixers for Studying Protein Folding
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Microfluidic Mixers for Studying Protein Folding

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Related Experiment Videos

Last Updated: Jun 11, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

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

Published on: February 12, 2019

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • Proteins can adopt multiple distinct fold topologies.
  • This structural plasticity expands protein functional capabilities through novel binding interactions.

Purpose of the Study:

  • To explore the common features and implications of protein fold switching.
  • To understand how amino acid sequences encode latent functional states.

Main Methods:

  • Analysis of naturally occurring and designed protein systems exhibiting fold switching.
  • Identification of common characteristics in structural transitions.

Main Results:

  • Fold switching necessitates transient states of reduced stability.
  • Flexible regions are crucial for conformational transitions.
  • Alternative folds expose new binding surfaces, enhancing stability and function.

Conclusions:

  • Protein fold switching offers insights into the evolution of protein folds.
  • Amino acid sequences possess greater information content, encoding multiple functional conformations.