Characterization of Protein Interactions in Eye Lens Crystallin Proteins and Crystallization

The central theme of this research is to understand how protein interactions alter the state of aggregation and the characterization of these interactions through light scattering properties of dense suspensions. One context where protein interactions have an impact on the state of aggregation is in protein crystallization. Crystallization of globular macromolecules is a difficult process. Often identification of the conditions resulting in X-ray quality crystals involves a large number of trial experiments where several solution conditions are screened. This process is slow, tedious and provides little assurance that crystallization conditions are found. In addition, screening processes provide no insights into why certain conditions work with some globular macromolecules and not with others. Crystallization occurs when an ordered dense packing of the protein has a lower free energy than a disordered amorphous solution. This is accomplished by increasing the protein concentration and increasing the strength of attractions. In this work, the development of a convenient method that provides guidance towards these necessary steps for crystallization is discussed.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Mirarefi, Amir Y.

Contributors dc:contributor

• Zukoski, Charles F.

• Biophysics, General

Language dc:language

eng

Identifier

(MiAaPQ)AAI3199090

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/87909