General Features of Ligand Binding to Heme Proteins
Yue, Kwok To
This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.
Permalink
https://hdl.handle.net/2142/77477
Description
Title
General Features of Ligand Binding to Heme Proteins
Author(s)
Yue, Kwok To
Issue Date
1983
Department of Study
Center for Biophysics and Computational Biology
Discipline
Biophysics
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biophysics, General
Language
eng
Abstract
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.
Use this login method if you
don't
have an
@illinois.edu
email address.
(Oops, I do have one)
IDEALS migrated to a new platform on June 23, 2022. If you created
your account prior to this date, you will have to reset your password
using the forgot-password link below.
