title: Zaccai neutron resilience and site-specific hydration dynamics in a globular protein.
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.
authors.affiliation: University of Tennessee/Oak Ridge National Laboratory Center for Molecular Biophysics, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
authors.forename: Yinglong
authors.initials: Y
authors.lastname: Miao
authors.forename: Liang
authors.initials: L
authors.lastname: Hong
authors.forename: Zheng
authors.initials: Z
authors.lastname: Yi
authors.forename: Jeremy C
authors.initials: JC
authors.lastname: Smith
mesh_terms: D000595:Amino Acid Sequence; D019475:Camphor 5-Monooxygenase / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D033363:Neutron Diffraction; D017434:Protein Structure, Tertiary; D053838:Scattering, Small Angle; D014867:Water / Q000737:chemistry
chemical_list: D014867:Water; D019475:Camphor 5-Monooxygenase