Effects of Immobilization Matrices and Protein Orientation on Biomolecular Recognition at Solid-Liquid Interfaces

The specific recognition between biological molecules has been widely exploited in many applications in medicine, biology, and biotechnology. These applications range from biosensors to affinity chromatography. However, the immobilization of biomolecules, such as proteins, often results in the loss of their biological activities. Factors that impact the apparent kinetics and affinities of the biomolecular interactions at the solid-liquid interfaces were examined with a combination of several physical techniques. The recognition between cytochrome b5 and cytochrome c was chosen as the model system to both identify and quantify the forces that originated from the immobilization substrates and the protein immobilization orientations. These measured forces were correlated with the measured kinetics and affinities of the recognition of immobilized proteins by their binding partners.

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

2015

Author dc:creator

• Yeung, Chiuman

Contributors dc:contributor

• Leckband, Deborah E.

• Engineering, Chemical
• Biophysics, General

Language dc:language

eng

Identifier

(UMI)AAI9904632

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/77478