Developing Novel Non-Natural Amino Acids as Spectroscopic Reporters of Structure for Peptide Systems

Properly folded proteins are essential to living organisms. Mis-folded proteins can lead to some serious diseases such as Alzheimer's disease, Lou Gehrig's disease (ALS), and muscular dystrophy which affect many people. The key to potentially preventing such diseases lies in understanding how and why protein mis-folding occurs and determining ways to prevent it from happening in the first place. This thesis describes a possible method of determining how proteins fold in solution using vibrational probes, two types of infrared spectroscopy (Fourier Transform Infrared and two-dimensional infrared), and molecular dynamics simulations. With these three techniques, the angle, distance, and coupling constant between vibrational probes can be determined. These three quantities allow for the determination of orientation of the backbone of each peptide or protein as well as the orientation of the probes within the peptide or protein systems in solution. These studies lay the groundwork for technical advances in monitoring protein folding in solution on the femtosecond timescale.

Level thesis:degree_level

Master's Degree

Year dc:date.issued

2018

Author dc:creator

• Cunningham, Amy

Advisor dc:contributor.advisor

• Tucker, Matthew J.

Committee members dc:contributor.committeemember

• Geary, Laina M
• Wallace, Ian S

• Infrared
• Peptide
• Spectroscopy
• Vibrational Probes

Statement dc:rights

• Creative Commons Attribution-NoDerivatives 4.0 United States

Handle dc:identifier.uri

http://hdl.handle.net/11714/4549

OAI identifier oai:identifier

oai:scholarwolf.unr.edu:11714/4549