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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...
Amyloid Fibrils03:03

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, normally used to...

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Updated: Jun 14, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Protein folding sculpting evolutionary change.

S Lindquist1

  • 1Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, MA 02142, USA. lindquist_admin@wi.mit.edu

Cold Spring Harbor Symposia on Quantitative Biology
|April 9, 2010
PubMed
Summary
This summary is machine-generated.

Protein folding, regulated by molecular chaperones like Hsp90, influences how genetic changes become observable traits, driving evolutionary adaptation. This study reveals mechanisms where Hsp90 and prions facilitate rapid evolution in response to environmental changes.

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Area of Science:

  • Evolutionary Biology
  • Molecular Biology
  • Genetics

Background:

  • Protein folding is crucial for translating genotypes into phenotypes.
  • Molecular chaperones, such as heat-shock proteins (Hsps), ensure correct protein folding.
  • Hsp90 is a key chaperone for metastable signal transducers, influencing biological processes.

Purpose of the Study:

  • To define mechanisms by which Hsp90 influences the acquisition of new phenotypes.
  • To explore the role of protein folding in evolutionary processes.
  • To investigate the impact of environmental factors on Hsp90 client protein folding and trait evolution.

Main Methods:

  • Investigated Hsp90's role in buffering mutations and potentiating genetic variation.
  • Examined the influence of environmental stress on Hsp90 function and phenotype expression.
  • Studied prion-based hereditary elements as another mechanism linking protein folding to evolution.

Main Results:

  • Hsp90 buffers mutations, storing cryptic genetic variation released by stress, leading to new traits.
  • Hsp90 potentiates genetic variation, enabling immediate phenotypes, and can facilitate trait assimilation.
  • Prions induce heritable phenotypic changes via protein conformation, influenced by environmental stress and genetic variation.

Conclusions:

  • Protein folding forces significantly impact genotype-phenotype translation and evolution.
  • Hsp90 and prions offer mechanisms coupling environmental changes to evolutionary innovation.
  • These findings provide a new paradigm for rapid, stepwise evolution and potential therapeutic strategies.