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Ohara, Takashi; Umino, Hisao; Tamada, Taro; Kuroki, Ryota
no journal, ,
no abstracts in English
Ohara, Takashi; Umino, Hisao; Tamada, Taro; Kuroki, Ryota
no journal, ,
no abstracts in English
Ohara, Takashi; Tamada, Taro; Adachi, Motoyasu; Kuroki, Ryota; Umino, Hisao*
no journal, ,
no abstracts in English
Okazaki, Nobuo; Ohara, Takashi; Umino, Hisao*; Chatake, Toshiyuki*; Kurihara, Kazuo; Cachau, R. E.*; Blaber, M.*; Niimura, Nobuo*; Kuroki, Ryota
no journal, ,
Okazaki, Nobuo; Ohara, Takashi; Umino, Hisao*; Chatake, Toshiyuki*; Kurihara, Kazuo; Cachau, R. E.*; Blaber, M.*; Niimura, Nobuo*; Kuroki, Ryota
no journal, ,
In protein molecules, key energetic contributors are solvation, desolvation and hydrogen bonding. They contribute protein folding, dynamics and molecular recognition. As a result, more elaborate studies of hydrogen atoms will be great help to recognize protein structures and obtain new findings of them. However, we do not have system which dedicated to characterization and analysis of hydrogen bonding. Therefore, we have developed a database for hydrogen and hydration water molecules. That database named Hydrogen and Hydration Database for Biomolecules (HHDB). Hydrogen bond data stored to HHDB use hydrogen atom coordinates determined directly by neutron diffraction and certain extremely high resolution X-ray diffraction. HHDB provides graphical user interface, users can use it through web browser. HHDB can visualize hydrogen atom positions in protein and solvent, and hydrogen bonding interactions. Fig. 1 shows HHDB plot example. In this plot, hydrogen atom is placed at the origin, and each point represents hydrogen bond distance and angle. We are improving the web user interfaces and the performance for usability.