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Ability of thrombin to act as molecular chaperone, inducing formation of quadruplex structure of thrombin-binding

Eva Baldrich1, Ciara K O'Sullivan

  • 1Department of Chemical Engineering, Universitat Rovira Virgili, Avinguda Països Catalans 26, 43007 Tarragona, Spain.

Analytical Biochemistry
|May 4, 2005
PubMed
Abstract

No abstract available in PubMed .

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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.
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