Decomposition of total solvation energy into core, side-chains and water contributions: Role of cross correlations and protein conformational fluctuations in dynamics of hydration layer

Mondal, Sayantan and Mukherjee, Saumyak and Bagchi, Biman (2017) Decomposition of total solvation energy into core, side-chains and water contributions: Role of cross correlations and protein conformational fluctuations in dynamics of hydration layer. In: CHEMICAL PHYSICS LETTERS, 683 . pp. 29-37.

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Abstract

Dynamical coupling between water and amino acid side-chain residues in solvation dynamics is investigated by selecting residues often used as natural probes, namely tryptophan, tyrosine and histidine, located at different positions on protein surface. Such differently placed residues are found to exhibit different timescales of relaxation. The total solvation response measured by the probe is decomposed in terms of its interactions with (i) protein core, (ii) side-chain and (iii) water. Significant anti cross-correlation among these contributions are observed. When the motion of the protein side-chains is quenched, solvation either becomes faster or slower depending on the location of the probe. (C) 2017 Elsevier B.V. All rights reserved.

Item Type:	Journal Article
Publication:	CHEMICAL PHYSICS LETTERS
Additional Information:	Copy right for this article belongs to the ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
Department/Centre:	Division of Chemical Sciences > Solid State & Structural Chemistry Unit
Date Deposited:	12 Aug 2017 04:09
Last Modified:	12 Aug 2017 04:09
URI:	http://eprints.iisc.ac.in/id/eprint/57595

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