Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
Volume 44 , Issue 3
Issue 253
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  • Naoya SHIBAYAMA
    2004 Volume 44 Issue 3 Pages 108-112
    Published: 2004
    Released: May 21, 2004
    JOURNALS FREE ACCESS
    The binding of ligands by proteins is accompanied by rapid structural changes that are essential to function. A recent crystallographic study has revealed the ligation-linked protein motions in an allosteric protein, human hemoglobin, in both allosteric forms (T and R) upon photolysis of bound CO at cryogenic temperatures. The results show how differently the α and β subunits, within each allosteric form, respond to loss of ligand, and where the free ligand lies, establishing that the mechanism of protein control of ligand binding is radically different between the subunits.
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  • Mikihiro SHIBATA, Hideki KANDORI
    2004 Volume 44 Issue 3 Pages 113-117
    Published: 2004
    Released: May 21, 2004
    JOURNALS FREE ACCESS
    Internal water molecules are considered to play a crucial role in the functional processes of ion pump proteins, though little has been known about their structure and function. We have studied hydrogen-bonding alterations of internal water molecules in a light-driven proton pump, bacteriorhodopsin, by means of low-temperature Fourier-transform infrared (FTIR) spectroscopy. Highly accurate measurements enabled us to detect even a single stretching vibration of such water molecules. In addition, analysis of the water molecules hydrating with negative charges led to a proposal of the "hydration switch model" for the primary proton transfer reaction in bacteriorhodopsin.
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