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

We then investigated the dependence of protein orientation on the forces between immobilized proteins and soluble ligands. Oriented cytochrome b5 monolayers were constructed on supported lipid membranes using a site-selective immobilization method. The orientation of the immobilized cytochrome b5 was well controlled as verified with linear dichroism measurements. The orientational dependence of the protein electrostatic surface potentials was observed by direct force measurement. The impact of immobilized cytochrome b5 orientation on the forces mediating the cytochrome b5-cytochrome c recognition was quantified, and correlated with the measured surface binding behaviors. We found good agreement between force measurements, molecular models, and equilibrium binding behavior.

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

• Yeung, Chiuman

Contributors dc:contributor

• Leckband, Deborah E.

• Biophysics, General

Language dc:language

eng

Identifier

(MiAaPQ)AAI9904632

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/87869