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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

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Protein Folding01:22

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Molecular Chaperones and Protein Folding03:00

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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.
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 Organization01:13

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Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Engineering a two-helix bundle protein for folding studies.

Charlotte A Dodson1, Neil Ferguson, Trevor J Rutherford

  • 1MRC Centre for Protein Engineering, Hills Road, Cambridge CB20QH, UK.

Protein Engineering, Design & Selection : PEDS
|February 5, 2010
PubMed
Summary
This summary is machine-generated.

Researchers engineered a Saccharomyces cerevisiae THO1 protein SAP domain mutant (L31W) for protein folding studies. This engineered protein exhibits reversible, two-state folding kinetics, making it suitable for further investigation into protein dynamics.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • The SAP domain of Saccharomyces cerevisiae THO1 protein features a hydrophobic core and two alpha-helices.
  • This domain presents a model system for protein folding studies, bridging research on isolated helices and larger protein domains.

Purpose of the Study:

  • To engineer the SAP domain for enhanced protein folding studies.
  • To investigate the structural and folding properties of a mutated SAP domain (L31W).

Main Methods:

  • Engineering of the SAP domain by introducing a tryptophan residue at position 31 (L31W).
  • Structure determination of the engineered SAP domain.
  • Analysis of protein folding kinetics and stability.

Main Results:

  • The L31W mutation resulted in a backbone root mean-squared deviation of 0.9 Å for helical regions compared to wild type.
  • The L31W mutation destabilized the wild-type protein by 0.8 ± 0.1 kcal mol⁻¹.
  • The mutant protein demonstrated reversible, apparent two-state folding with a folding rate constant of approximately 3700 s⁻¹.

Conclusions:

  • The engineered L31W SAP domain mutant is suitable for detailed protein folding studies.
  • This mutant provides a valuable tool for understanding the fundamental principles of protein folding mechanisms.