Protein dynamics: hydration and cavities

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 t...

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Main Author:	K. Heremans
Format:	Article
Language:	English
Published:	Associação Brasileira de Divulgação Científica 2005-08-01
Series:	Brazilian Journal of Medical and Biological Research
Subjects:	Stability diagram Thermodynamics High pressure Unfolding Amyloid fibrils Protein dynamics
Online Access:	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800002

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spelling	doaj-44be071dc7634803a745cd9561ccefcf2020-11-25T00:56:35ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2005-08-013881157116510.1590/S0100-879X2005000800002Protein dynamics: hydration and cavitiesK. HeremansThe 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800002Stability diagramThermodynamicsHigh pressureUnfoldingAmyloid fibrilsProtein dynamics
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	K. Heremans
spellingShingle	K. Heremans Protein dynamics: hydration and cavities Brazilian Journal of Medical and Biological Research Stability diagram Thermodynamics High pressure Unfolding Amyloid fibrils Protein dynamics
author_facet	K. Heremans
author_sort	K. Heremans
title	Protein dynamics: hydration and cavities
title_short	Protein dynamics: hydration and cavities
title_full	Protein dynamics: hydration and cavities
title_fullStr	Protein dynamics: hydration and cavities
title_full_unstemmed	Protein dynamics: hydration and cavities
title_sort	protein dynamics: hydration and cavities
publisher	Associação Brasileira de Divulgação Científica
series	Brazilian Journal of Medical and Biological Research
issn	0100-879X 1414-431X
publishDate	2005-08-01
description	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.
topic	Stability diagram Thermodynamics High pressure Unfolding Amyloid fibrils Protein dynamics
url	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800002
work_keys_str_mv	AT kheremans proteindynamicshydrationandcavities
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Protein dynamics: hydration and cavities

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