Eur. Phys. J. E (2013) 36: 72
https://doi.org/10.1140/epje/i2013-13072-5

Regular Article

Zaccai neutron resilience and site-specific hydration dynamics in a globular protein

¹⁹⁸⁸⁵ Oak Ridge National Laboratory, University of Tennessee/Oak Ridge National Laboratory Center for Molecular Biophysics, 37831, Oak Ridge, TN, USA
²⁹⁸⁸⁵ Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee-Knoxville, 37996, Knoxville, TN, USA

^* e-mail: smithjc@ornl.gov

Received: 26 September 2012
Revised: 18 January 2013
Accepted: 20 February 2013
Published online: 16 July 2013

Abstract

A discussion is presented of contributions of the Zaccai group to the understanding of flexibility in biological macromolecules using dynamic neutron scattering. The concept of resilience as introduced by Zaccai is discussed and investigated using molecular dynamics simulation on camphor-bound cytochrome P450. The resilience of hydrophilic residues is found to be more strongly affected by hydration than that of hydrophobic counterparts. The hydration-induced softening of protein propagates from the surface into the dry core. Moreover, buried hydrophilic residues behave more like those exposed on the protein surface, and are different from their hydrophobic counterparts.