Rate-window methods and myoglobin dynamics

The problem of protein dynamics is introduced and its significance explained. Properties of the oxygen-storage protein myoglobin (Mb) as a model system for dynamics studies are discussed. Special attention is paid to Mb's physiological role, and the basic quantities that describe the protein's function. Background on ligand binding experiments in Mb is reviewed and appropriate mathematical models established. The specific goal of this work is to determine as many as possible of the model parameters (pre-exponentials and activation enthalpies of intrinsic rate coefficients), with a view towards calculation of one functionally important quantity, the CO affinity at physiological temperatures.

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

2011

Author dc:creator

• Berendzen, Joel Ray

Contributors dc:contributor

• Frauenfelder, Hans

• Chemistry, Biochemistry
• Chemistry, Physical
• Biophysics, General

Statement dc:rights

• Copyright 1990 Berendzen, Joel Ray

Language dc:language

eng

Identifier

AAI9026138
(UMI)AAI9026138

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/21296