Data/hora: 05/06/2024 08:07:08

Provedor de dados: | 56
País: | Brazil
Título: | The powerful high pressure tool for protein conformational studies
Autores: | Marchal,S.; Torrent,J.; Masson,P.; Kornblatt,J.M.; Tortora,P.; Fusi,P.; Lange,R.; Balny,C.
Data: | 2005-08-01
Ano: | 2005
Palavras-chave: | High pressure; Prion protein; Amyloid; Ataxin; Enolase; Butyrylcholinesterase.
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 2º, 3º and 4º 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.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004
Editor: | Associação Brasileira de Divulgação Científica
Relação: | 10.1590/S0100-879X2005000800004
Formato: | text/html
Fonte: | Brazilian Journal of Medical and Biological Research  v.38 n.8 2005
Fonte: | info:eu-repo/semantics/openAccess