Stoructural science and various functions in hydorogen-bond materials. Hydration Structures of Protein Molecules Revealed by Cryogenic X-ray Crystallography.

• NAKASAKO Masayoshi

  PRESTO, JST and Molecular and Cellular Biosciences, The University of Tokyo

Bibliographic Information

Other Title

• 水素結合における構造物性と機能　　蛋白質の水和構造
• タンパクシツ ノ スイワ コウゾウ

Abstract

Hydration structures surrounding protein molecules have great influences on folding, stability, physical properties and functions of the molecules. In spite of this fact, X-ray protein crystallography have not sufficiently contributed on hydration structure analyses of proteins. Recent progress in cryogenic techniques enables us to analyze hydration structures of proteins. Cryogenic analyses have provided the structural information on hydration patterns around hydrophobic residues and network structures formed by hydration water molecules. New insights into the hydration structures of proteins have been given by cryogenic X-ray crystallography.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 40 (1), 107-113, 1998

  The Crystallographic Society of Japan

Details

• CRID: 1390282679063126400
• NII Article ID: 10002590445
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.40.107
• COI: 1:CAS:528:DyaK1cXit12hu7g%3D
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 4446296
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I4446296
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed