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|Type:||Artigo de periódico|
|Title:||Conformational Changes in Human Hsp70 Induced by High Hydrostatic Pressure Produce Oligomers with ATPase Activity but without Chaperone Activity|
|Abstract:||We investigated the folding of the 70 kDa human cytosolic inducible protein (Hsp70) in vitro using high hydrostatic pressure as a denaturing agent. We followed the structural changes in Hsp70 induced by high hydrostatic pressure using tryptophan fluorescence, molecular dynamics, circular dichroism, high-performance liquid chromatography gel filtration, dynamic light scattering, ATPase activity, and chaperone activity. Although monomeric, Hsp70 is very sensitive to hydrostatic pressure; after pressure had been removed, the protein did not return to its native sate but instead formed oligomeric species that lost chaperone activity but retained ATPase activity.|
|Editor:||Amer Chemical Soc|
|Appears in Collections:||Artigos e Materiais de Revistas Científicas - Unicamp|
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