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Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
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How well can fragments explore accessed chemical space? A case study from heat shock protein 90

Stephen D Roughley1, Roderick E Hubbard

  • 1Vernalis (R&D) Ltd., Granta Park, Abington, Cambridge, CB21 6GB, UK.

Journal of Medicinal Chemistry
|May 13, 2011
PubMed
Abstract

No abstract available in PubMed .

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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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