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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|
Oliveira Junior R.S.
|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. © 2014 American Chemical Society.|
|Editor:||American Chemical Society|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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