Journal of Biological Physics

, Volume 28, Issue 2, pp 129–137

Structural Characteristics in Protein Hydration Investigated by Cryogenic X-ray Crystal Structure Analyses

  • Masayoshi Nakasako
Article

DOI: 10.1023/A:1019982220615

Cite this article as:
Nakasako, M. Journal of Biological Physics (2002) 28: 129. doi:10.1023/A:1019982220615

Abstract

Cryogenic X-ray crystallography has heen applied to investigate thehydration structures of proteins. The amount of hydration water moleculesidentified at cryogenic temperature is more than twice those at ambienttemperature, and the structural models of proteins with a lot of hydrationwater molecules have provided much information to elucidate the static anddynamical characteristics of hydration structures of proteins. On proteinsurface, hydration water molecules distribute non-randomly and stillretain the tetrahedral hydrogen-bond geometry as well as in bulk solvent.In addition, water molecules form clathrate-like arrangements to cover thehydrophobic residues exposed to solvent. The standard interaction geometryenables the three-dimensional extension of hydrogen-bond networks aroundprotein molecules and, simultaneously, ensures the concerted reorganizationof hydration structures during the dynamical motion of proteins at work.The hydration structure analyses at cryogenic temperatures may contributeto understanding physical principles governing the dynamics of `molecularmachines' in aqueous environment.

cryogenic X-ray crystallography hydrogen bond protein dynamics protein hydration water molecule 

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Masayoshi Nakasako
    • 1
  1. 1.Department of Physics, Faculty of Science and EngineeringKeio University and PRESTO-JSTKohoku-ku, Yokohama, KanagawaJapan

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