Abstract

A general monomer-dimer equilibrium system involving ligand interactions is presented. Cooperativity features of specific limited models are analyzed by selecting the appropriate family of equilibrium constants from this general scheme. Each system is then characterized in terms of Hill coefficient dependency on alterations in values of equilibrium constants and total acceptor concentration. This method permits comparison of predicted cooperativity trends between systems. Contrasting reports concerning cooperativity dependencies for certain defined equilibrium systems are compared and the discrepancies resolved. Characteristics of cooperativity binding patterns are shown to include symmetry about dimerization association constant values, both positive and negative cooperativity for a single set of parameters, and significant changes in cooperativity features with relatively small changes in equilibrium parameters.

LLU Discipline

Biochemistry

Department

Biochemistry

School

Graduate School

First Advisor

W. Barton Rippon

Second Advisor

Charles W. Slattery

Third Advisor

R. Bruce Wilcox

Degree Name

Master of Science (MS)

Year Degree Awarded

1986

Date (Title Page)

6-1986

Language

English

Library of Congress/MESH Subject Headings

Ligands; Equilibrium; Binding Sites; Proteins -- analysis

Type

Thesis

Page Count

ill; 38

Digital Format

PDF

Digital Publisher

Loma Linda University Libraries

Usage Rights

This title appears here courtesy of the author, who has granted Loma Linda University a limited, non-exclusive right to make this publication available to the public. The author retains all other copyrights.

Collection

Loma Linda University Electronic Theses and Dissertations

Collection Website

http://scholarsrepository.llu.edu/etd/

Repository

Loma Linda University. Del E. Webb Memorial Library. University Archives

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Included in

Biochemistry Commons

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