Journal
CHEMICAL PHYSICS
Volume 420, Issue -, Pages 35-43Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.chemphys.2013.04.019
Keywords
Molecular simulation; Protein; Hydration; Surface water
Funding
- Department of Science and Technology (DST), Government of India [SR/S1/PC-23/2007]
- DST-FIST programme [SR/FST/CSII-011/2005]
- Council for Scientific and Industrial Research (CSIR), New Delhi
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Protein-water interactions and their influence on surrounding water is a long-standing problem. Despite its importance, the origin of differential water behavior at the protein surface is still elusive. We have performed molecular simulations of the protein barstar in aqueous medium. Efforts have been made to explore how the conformational motions of the protein segments in the native form and the heterogeneous electrostatic interactions with the polar and charged groups of the protein affect the interfacial water properties. The calculations reveal that reduced dimension of the hydration layer on freezing the protein's degrees of freedom does not modify the heterogeneous water distributions around the protein. However, turning off the protein-water electrostatic contribution leads to non-preferential near-uniform water arrangements at the surface. It is further shown that with protein-water electrostatic interactions turned on, the local structuring of water molecules around the segments are correlated with their degree of exposure to the solvent. (C ) 2013 Elsevier B. V. All rights reserved.
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