Data/hora: 28/05/2024 16:39:44

Provedor de dados: | Brazilian Journal of Medical and Biological Research
País: | Brazil
Título: | Protein dynamics: hydration and cavities
Autores: | Heremans,K.
Data: | 2005-08-01
Ano: | 2005
Palavras-chave: | Stability diagram; Thermodynamics; High pressure; Unfolding; Amyloid fibrils; Protein dynamics.
Resumo: | The temperature-pressure behavior of proteins seems to be unique among the biological macromolecules. Thermodynamic as well as kinetic data show the typical elliptical stability diagram. This may be extended by assuming that the unfolded state gives rise to volume and enthalpy-driven liquid-liquid transitions. A molecular interpretation follows from the temperature and the pressure dependence of the hydration and cavities. We suggest that positron annihilation spectroscopy can provide additional quantitative evidence for the contributions of cavities to the dynamics of proteins. Only mature amyloid fibrils that form from unfolded proteins are very resistant to pressure treatment.
Tipo: | Info:eu-repo/semantics/article
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800002
Editor: | Associação Brasileira de Divulgação Científica
Relação: | 10.1590/S0100-879X2005000800002
Formato: | text/html
Fonte: | Brazilian Journal of Medical and Biological Research  v.38 n.8 2005
Fonte: | info:eu-repo/semantics/openAccess