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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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Related Experiment Video

Updated: Jun 22, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Evaluating beta-turn mimics as beta-sheet folding nucleators.

Amelia A Fuller1, Deguo Du, Feng Liu

  • 1Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 23, 2009
PubMed
Summary
This summary is machine-generated.

Beta-turn mimics can act as protein folding nucleators, accelerating the formation of beta-sheets. Researchers classified these mimics based on their ability to initiate and speed up protein folding.

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Last Updated: Jun 22, 2026

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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Folding Dynamics
  • Structural Biology

Background:

  • Beta-turns are crucial protein conformations for globular structure formation and often represent rate-limiting steps in protein folding.
  • Beta-turn mimics are designed to replace specific amino acid residues, potentially acting as folding nucleators by preorganizing polypeptide chains.

Purpose of the Study:

  • To kinetically investigate the role of beta-turn mimics as nucleators in the context of a cooperatively folding protein.
  • To classify beta-turn mimics based on their impact on protein folding rates and nucleation capacity.

Main Methods:

  • Incorporation of six distinct beta-turn mimics into an engineered beta-turn or beta-bulge turn of the Pin 1 WW domain.
  • Kinetic experiments to measure alterations in beta-sheet folding rates.
  • Solution Nuclear Magnetic Resonance (NMR) to determine the structural integrity of the protein with incorporated mimics.

Main Results:

  • Beta-turn mimics were classified into three categories: weak nucleators, native-like nucleators, and strong nucleators.
  • Strong nucleators significantly accelerated protein folding rates compared to controls.
  • Incorporation of a strong E-olefin nucleator did not disrupt the native beta-sheet structure of the Pin 1 WW domain, as confirmed by NMR.

Conclusions:

  • Beta-turn mimics can function as effective protein folding nucleators, with varying capacities.
  • The developed kinetic analyses provide a method to assess the nucleation potential of beta-turn mimics.
  • These mimics offer a tool for studying protein folding transition state structures.