Macromolecular unfolding properties in presence of compatible solutes

We present Molecular Dynamics simulations of Chymotrypsin inhibitor II and PEO in presence of compatible solutes. Our results indicate that the the native compact state of the studied macromolecules is stabilized in presence of hydroxyectoine. We are able to explain the corresponding mechanism by a...

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Bibliographic Details
Published in:arXiv.org 2011-10
Main Authors: Smiatek, Jens, Galla, Hans-Joachim, Heuer, Andreas
Format: Article
Language:English
Subjects:
Chymotrypsin
Free energy
Macromolecules
Molecular dynamics
Online Access:Get full text
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Summary:We present Molecular Dynamics simulations of Chymotrypsin inhibitor II and PEO in presence of compatible solutes. Our results indicate that the the native compact state of the studied macromolecules is stabilized in presence of hydroxyectoine. We are able to explain the corresponding mechanism by a variation of the solvent properties for higher hydroxyectoine concentrations. Our results are validated by detailed free energy calculations.
ISSN:2331-8422