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Frauenfelder, Hans Bagley, Kimberly Ann 2011-06-02T14:38:59Z 2011-06-02T14:38:59Z 10000-01-01 1987 Fourier-transform infrared difference spectroscopy has been used to detect the vibrational modes of the chromophore and protein that change in position and intensity between rhodopsin and the photoproducts formed at low temperature (70K), bathorhodopsin and isorhodopsin. A method has been developed to obtain infrared difference spectra between rhodopsin and bathorhodopsin, bathorhodopsin and isorhodopsin, and rhodopsin and isorhodopsin. To aid in identification of the vibrational modes, experiments were performed on deuterated and hydrated films of native rod outer segments and rod outer segments regenerated with either retinal containing 13c at carbon-15 or 15-deuterioretinal, or hydrated films of rod outer segments regenerated with retinal containing 13c at either carbon-10, carbon-11, carbon-13, or carbons-14 and -15. These infrared studies provide independent verification of the resonance Raman result that the retinal in bathorhodopsin is all-trans-like. The positions of the C=N stretch in the deuterated pigment and the deuterated pigments regenerated with 11-cis 15-deuterioretinal or 11-cis retinal containing 13c at carbon-15 are indicative that the Schiff base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin. Furthermore, the C=N stretching frequency occurs at the same position in all three species. The data indicate that the protonated Schiff base has a C=N trans conformation in all three species, and that the ClO-Cll single bond is s-trans in bathorhodopsin. Finally, evidence is presented that, even in these early stages of the rhodopsin bleaching sequence, changes are occurring in the-opsin. Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-02T14:38:59Z No. of bitstreams: 1 1987_Bagley.pdf: 1366649 bytes, checksum: ee92c0e8993dd9c5bf701892921ffd45 (MD5) Made available in DSpace on 2011-06-02T14:38:59Z (GMT). No. of bitstreams: 1 1987_Bagley.pdf: 1366649 bytes, checksum: ee92c0e8993dd9c5bf701892921ffd45 (MD5) Previous issue date: 1987 Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-02T14:38:59Z Item is restricted indefinitely. Restriction data tranferred 2014-07-01T11:11:25-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis Thesis U of I Only 1854058 http://hdl.handle.net/2142/25211 en 1987 Kimberly Ann Bagley Fourier-transform infrared difference spectroscopy vebrational modes chromophore rhodopsin bathorhodopsin isorhodopsin Infrared studies of rhodopsin and its low temperature photoproducts, bathorhodopsin and isorhodopsin Dissertation / Thesis text Physics Physics University of Illinois at Urbana-Champaign Dissertation Ph.D.