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Sligar, Stephen G. Carlson, Joseph Woodward 2015-09-28T22:11:45Z 2015-09-28T22:11:45Z 10000-01-01 1999 1999 In separate studies, myoglobin has been used to study the fluorescence lifetime behavior of oriented biomolecular surfaces. These studies have revealed differences in lifetime between differentially oriented myoglobin molecules, consistent with differential accessibility of the heme pocket to quenching by oxygen. A computational study of the dependence of linear dichroism on the distribution of protein orientation angle has revealed a constrained degenerate solution, which has impact on all attempts to describe protein orientation with this technique. Made available in DSpace on 2015-09-28T22:11:45Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9944810.pdf: 4237766 bytes, checksum: 9262a2f7eceb717534c3977a40904f31 (MD5) Previous issue date: 1999 Embargo set by: Seth Robbins for item 89196 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 101 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999. http://hdl.handle.net/2142/87915 (MiAaPQ)AAI9944810 eng Health Sciences, Pharmacology Supramolecular Architectures in Molecular Medicine: Visualizing and Manipulating the Structure of Protein-Lipid Surfaces text University of Illinois at Urbana-Champaign Dissertation Ph.D.