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Related Concept Videos

Protein Folding01:25

Protein Folding

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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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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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Protein Denaturation01:28

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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Updated: Apr 7, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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Why and How Does Pressure Unfold Proteins?

Catherine A Royer1

  • 1Department of Biology, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA, royerc@rpi.edu.

Sub-Cellular Biochemistry
|July 16, 2015
PubMed
Summary
This summary is machine-generated.

High hydrostatic pressure can denature proteins, a phenomenon known since 1914. Despite extensive research, the precise mechanism of pressure

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Protein Science

Background:

  • The 100th anniversary of the first report on protein denaturation by high hydrostatic pressure (HHP) was in 2014.
  • Research on pressure effects on protein stability has significantly increased.
  • The exact mechanisms by which HHP affects proteins are still debated.

Purpose of the Study:

  • To provide an overview of the current state of the debate on pressure effects on protein stability.
  • To synthesize recent findings and ongoing discussions in the field.

Main Methods:

  • Literature review of studies on pressure effects on protein stability.
  • Analysis of the mechanisms of protein denaturation by HHP.
  • Synthesis of the author's perspective on the current debate.

Main Results:

  • The field has seen a surge in studies investigating pressure-induced protein denaturation.
  • Significant debate persists regarding the precise molecular mechanisms involved.
  • A comprehensive overview of the current understanding and controversies is presented.

Conclusions:

  • Understanding the mechanism of pressure effects on proteins remains a key challenge.
  • Further research is needed to resolve the ongoing debates.
  • This review offers a perspective on the current standing of these scientific discussions.