| Summary: | "We have measured the transient absorption spectrum of photolyzed sperm whale carboxymyoglobin as a function of temperature and time after photolysis. Our measurements extend from 60K to 220K and from three microseconds to thirty seconds. We see an absorption band near 758 nm which is known as band VIII. Three microseconds after photolysis at 60K, the center of band VIII is 766 nm, red-shifted from the peak seen in deoxy myoglobin at this temperature. Band VIII shifts with time towards the deoxy value with a nonexponential time course. We conclude that this shift is caused by unrelaxed degrees of freedom in the protein at these temperatures. We present a model in which each protein has several ""blocking residues"" which relax following photolysis by surmounting enthalpy barriers which range from ten to fifty kJ/mol. These motions do not affect the rate of ligand rebinding." Submitted by Carolyn Mead (cmead2@illinois.edu) on 2011-06-07T14:27:14Z No. of bitstreams: 1 1984_bowne.pdf: 2168038 bytes, checksum: eb47cbb8d85ab46ec7d7f6cb30861937 (MD5) Made available in DSpace on 2011-06-07T14:27:14Z (GMT). No. of bitstreams: 1 1984_bowne.pdf: 2168038 bytes, checksum: eb47cbb8d85ab46ec7d7f6cb30861937 (MD5) Previous issue date: 1984 Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Carolyn Mead (cmead2@illinois.edu) on 2011-06-07T14:27:14Z Item is restricted indefinitely. Restriction data tranferred 2014-07-01T11:11:32-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: Thesis Thesis U of I Only
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