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oai:www.ideals.illinois.edu:2142/77477 2023-07-11 col_2142_5131 col_2142_14828 com_2142_5130 com_2142_14827 com_2142_14793 com_2142_8903

Yue, Kwok To 2015-05-13T15:47:09Z 2015-05-13T15:47:09Z 10000-01-01 1983 1983 The binding of ligands to heme proteins has been studied extensively in the past. A sequential barrier model was postulated. Using flash photolysis, various aspects of the model are studied in this work to give a better understanding of ligand binding. Binding from the pocket, as seen at low temperatures as process I, is examined under the influence of xenon binding, pH, high ligand concentration and Zn('++) ions. A new approach is developed to understand binding at physiological temperatures. The effect of solvent is examined with the new approach. The role of diffusion in binding is discussed. Support for a sequential model and the existence of conformational substates are presented. The effect of high ligand concentration on the kinetics is also investigated. Made available in DSpace on 2015-05-13T15:47:09Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 8310023.PDF: 2789100 bytes, checksum: 188691c6697fd31bf0e8ba9431f92bdf (MD5) Previous issue date: 1983 Embargo set by: Seth Robbins for item 78688 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 112 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1983. http://hdl.handle.net/2142/77477 (UMI)AAI8310023 eng Biophysics, General General Features of Ligand Binding to Heme Proteins text Center for Biophysics and Computational Biology Biophysics University of Illinois at Urbana-Champaign Dissertation Ph.D.