Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/199215
Type: Artigo de periódico
Title: Human Hsp70/hsp90 Organizing Protein (hop) D456g Is A Mixture Of Monomeric And Dimeric Species.
Author: Gonçalves, Danieli C
Gava, Lisandra M
Ramos, Carlos H I
Abstract: Hop is a tetratricopeptide repeat domain (TPR)-containing co-chaperone that is able to directly associate with both Hsp70 and Hsp90. Previous data showed that the TPR2A-domain is the primary site for dimerization and that the TPR2B-domain may also play a role in dimerization. We present Hop-D456G, a mutant within the TPR2B-domain, that is a mixture of monomeric and dimeric species.
Subject: Amino Acid Sequence
Chromatography, Gel
Circular Dichroism
Dimerization
Escherichia Coli
Heat-shock Proteins
Humans
Linear Models
Molecular Sequence Data
Mutation
Protein Subunits
Recombinant Proteins
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/19961430
Date Issue: 2010
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

Files in This Item:
File SizeFormat 
pmed_19961430.pdf567.55 kBAdobe PDFView/Open


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