University of Illinois at Urbana-Champaign
General Features of Ligand Binding to Heme Proteins
Abstract
dc:descriptionThe 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.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Biophysics
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Yue, Kwok To
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (UMI)AAI8310023
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/77477