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Marchal,S.; Torrent,J.; Masson,P.; Kornblatt,J.M.; Tortora,P.; Fusi,P.; Lange,R.; Balny,C.. |
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... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: High pressure; Prion protein; Amyloid; Ataxin; Enolase; Butyrylcholinesterase. |
Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004 |
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