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Published on: April 10, 2012

一种内在无序的蛋白质的折叠和结合:快速,但不是"扩散受限"

Joseph M Rogers1, Annette Steward, Jane Clarke

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.

Journal of the American Chemical Society
|January 11, 2013
PubMed
概括

内在失序蛋白 (IDP) 的结合并不总是以扩散为限. 折叠蛋白质的标准测试不适合评估IDP结合动力学,揭示了对蛋白质相互作用的新见解.

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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
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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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