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dc.creatorDurbin, S. M.en_US
dc.creatorZhang, C.en_US
dc.date.accessioned2008-07-15T13:20:12Z
dc.date.available2008-07-15T13:20:12Z
dc.date.issued2008en_US
dc.identifier2008-TH-09en_US
dc.identifier.urihttp://hdl.handle.net/1811/33165
dc.descriptionC. Zhang, and S. M. Durbin, J. Phys. Chem. B 110, 23607 (2006).en_US
dc.descriptionAuthor Institution: Department of Physics, Purdue University, West Lafayette; IN 47907en_US
dc.description.abstractTHz absorption was measured for the heme protein myoglobin as a function of water content from 3.6 to 98 percent water by weight, using a THz time-domain spectrometer. Even for dry protein the spectra were dominated by residual water content and predicted protein normal modes peaks were not seen, likely due to inhomogeneous broadening. Careful analysis revealed that the THz absorption per protein molecule increased significantly at the high water content limit, despite the expected decreased polarizability of biological water. This effect may be due to a suppression of protein-protein interactions as higher water concentration increases the mean distance between protein molecules}.en_US
dc.language.isoEnglishen_US
dc.publisherOhio State Universityen_US
dc.titleTHE ROLE OF WATER IN THZ ABSORPTION BY MYOGLOBINen_US
dc.typeArticleen_US


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