Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity.
Biochemistry
; 53(18): 2884-9, 2014 May 13.
Article
em En
| MEDLINE
| ID: mdl-24739062
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
/
Adenosina Trifosfatases
/
Chaperonas Moleculares
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Proteínas de Choque Térmico HSP70
/
Pressão Hidrostática
Limite:
Humans
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Brasil