| Registro completo |
| Provedor de dados: |
BJMBR
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| País: |
Brazil
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| Título: |
Protein dynamics: hydration and cavities
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| Autores: |
Heremans,K.
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| Data: |
2005-08-01
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| Ano: |
2005
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| Palavras-chave: |
Stability diagram
Thermodynamics
High pressure
Unfolding
Amyloid fibrils
Protein dynamics
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| 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.
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800002
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| Editor: |
Associação Brasileira de Divulgação Científica
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| Relação: |
10.1590/S0100-879X2005000800002
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Medical and Biological Research v.38 n.8 2005
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| Direitos: |
info:eu-repo/semantics/openAccess
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