The powerful high pressure tool for protein conformational studies
Braz. j. med. biol. res
;
38(8): 1175-1183, Aug. 2005.
Artigo
em Inglês
| LILACS
| ID: lil-405518
RESUMO
The pressure behavior of proteins may be summarized as a the pressure-induced disordering of their structures. This thermodynamic parameter has effects on proteins that are similar but not identical to those induced by temperature, the other thermodynamic parameter. Of particular importance are the intermolecular interactions that follow partial protein unfolding and that give rise to the formation of fibrils. Because some proteins do not form fibrils under pressure, these observations can be related to the shape of the stability diagram. Weak interactions which are differently affected by hydrostatic pressure or temperature play a determinant role in protein stability. Pressure acts on the 2°, 3° and 4° structures of proteins which are maintained by electrostatic and hydrophobic interactions and by hydrogen bonds. We present some typical examples of how pressure affects the tertiary structure of proteins (the case of prion proteins), induces unfolding (ataxin), is a convenient tool to study enzyme dissociation (enolase), and provides arguments to understand the role of the partial volume of an enzyme (butyrylcholinesterase). This approach may have important implications for the understanding of the basic mechanism of protein diseases and for the development of preventive and therapeutic measures.
Texto completo:
DisponíveL
Índice:
LILACS (Américas)
Assunto principal:
Estrutura Terciária de Proteína
/
Pressão Hidrostática
Limite:
Humanos
Idioma:
Inglês
Revista:
Braz. j. med. biol. res
Assunto da revista:
Biologia
/
Medicina
Ano de publicação:
2005
Tipo de documento:
Artigo
/
Congresso e conferência
/
Documento de projeto
País de afiliação:
Canadá
/
França
/
Itália
Instituição/País de afiliação:
Concordia University/CA
/
Unité d'Enzymologie/FR
/
Università di Milano-Bicocca/IT
/
Université Montpellier II/FR
Similares
MEDLINE
...
LILACS
LIS