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

  • Yinglong Miao
  • Liang Hong
  • Zheng Yi
  • Jeremy C. Smith
Regular Article
Part of the following topical collections:
  1. Neutron Biological Physics

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.

Graphical abstract

Keywords

Topical issue: Neutron Biological Physics 

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Copyright information

© EDP Sciences, SIF, Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Yinglong Miao
    • 1
    • 2
  • Liang Hong
    • 1
    • 2
  • Zheng Yi
    • 1
    • 2
  • Jeremy C. Smith
    • 1
    • 2
  1. 1.Oak Ridge National LaboratoryUniversity of Tennessee/Oak Ridge National Laboratory Center for Molecular BiophysicsOak RidgeUSA
  2. 2.Department of Biochemistry and Cellular and Molecular BiologyUniversity of Tennessee-KnoxvilleKnoxvilleUSA

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