Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 Å resolution
作者： Andreas Ostermann , Ichiro Tanaka , Niklas Engler , Nobuo Niimura , Fritz G Parak
DOI: 10.1016/S0301-4622(01)00255-1
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摘要: Abstract From the first days of protein neutron structure determination sperm whale myoglobin was an object under investigation [Nature 224 (1969) 143, J. Mol. Biol. 220 (1991) 381]. Nevertheless is still interest [Proc. Natl. Acad. Sci. USA 97 (2000) 3872]. The feasibility monochromatic diffractometer BIX-3 at JRR-3M reactor JAERI [J. Phys. Chem. Solids 60 (1999) 1623], to collect high-resolution diffraction data in a relatively short time stimulated us repeat structural myoglobin. metmyoglobin has been determined up resolution 1.5 A. hydrogen atoms were replaced part, by deuterium soaking crystals for more than 10 years D 2 O. A refinement all performed including individual mean square displacements and occupancies exchangeable protons backbone bonds. method described show clear negative scattering densities H atoms. Water molecules within on molecule surface are shown. exchangeability correlated with distribution flexibility.
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