Cooperativity of ligand binding as a function of monomer-dimer equilibrium Parameters and Acceptor Concentration

<p>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.</p>

Name thesis:degree_name

Master of Science (MS)

Level thesis:degree_level

Thesis

Discipline thesis:degree_discipline

Biochemistry

Year

1986

Author dc:creator

• Wolfer, George K.

Contributors dc:contributor

• W. Barton Rippon
• Charles W. Slattery
• R. Bruce Wilcox

• Biochemistry
• Ligands; Equilibrium; Binding Sites; Proteins -- analysis

Statement dc: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.

Language dc:language

English

Repository record dc:identifier

https://scholarsrepository.llu.edu/etd/835

OAI identifier oai:identifier

oai:scholarsrepository.llu.edu:etd-1929