Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/87501
Type: Artigo de periódico
Title: Conformational Changes In Human Hsp70 Induced By High Hydrostatic Pressure Produce Oligomers With Atpase Activity But Without Chaperone Activity
Author: Araujo T.L.S.
Borges J.C.
Ramos C.H.
Meyer-Fernandes J.R.
Oliveira Junior R.S.
Pascutti P.G.
Foguel D.
Palhano F.L.
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
Rights: fechado
Identifier DOI: 10.1021/bi500004q
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84900531605&partnerID=40&md5=c61a2717c4be862a1bf3df63827e442d
Date Issue: 2014
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.