Date Thesis Awarded

5-2015

Access Type

Honors Thesis -- Access Restricted On-Campus Only

Degree Name

Bachelors of Science (BS)

Department

Chemistry

Advisor

Douglas Young

Committee Members

Lisa Landino

Matthew Wawersik

Kristin Wustholz

Abstract

Proteins are nature’s catalysts and have evolved over millennia to be highly selective and efficient. As a result, many have sought to incorporate proteins into artificial systems to varying degrees of success. Immobilization of proteins onto solid supports can increase the stability of proteins in conditions that would normally induce denaturation but immobilization strategies can present their own challenges by using reactions that lack selectivity and can potentially disrupt protein function themselves. This work develops a new methodology for protein immobilization that uses an unnatural amino acid site-selectively incorporated into a protein as the functional handle for immobilization. As a model system, Green Fluorescent Protein was immobilized in this manner and found to retain its functional activity in conditions which would normally cause the protein to denature. Through the development of this methodology, it was found that immobilization efficiency is affected by the site where the functional handle is inserted, in addition to the accessibility and reactivity of the solid support. Finally, progress was made towards determining whether this methodology can be successfully incorporated into a system which utilizes microwave irradiation.

Recommended Citation

Raliski, Benjamin K., "Development of a Site-Selective Protein Immobilization Methodology Utilizing Unnatural Amino Acids" (2015). Undergraduate Honors Theses. William & Mary. Paper 151.
https://scholarworks.wm.edu/honorstheses/151