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在单个分子层面上探测过渡性铜沙佩龙-威尔逊病蛋白相互作用,使用纳米微粒捕获

Jaime J Benítez1, Aaron M Keller, Patrick Ochieng

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.

Journal of the American Chemical Society
|February 6, 2008
PubMed
概括

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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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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