Validation of Theoretical IR Spectroscopic Methods for Protein Structure Determination

Student Author(s)

Yong Chul Yoon

Faculty Mentor(s)

Dr. Justin Shorb , Chemistry

Document Type


Event Date



Determination of the protein structure has become an increasingly important task for many scientists and pharmacists as the structure of a protein determines its function. For instance, many of the debilitating effects of genetic diseases are caused by the misfolding of proteins. Scientists have developed many different methods, such as X-ray crystallography and NMR, to characterize the structure of proteins. A more recent development in protein characterization involves the use of IR spectroscopy because we are able to capture the motion of proteins at physiological pH, and use isotope labeling to identify individual peptide linkages, which we cannot with other methods. Various groups have used theoretical models to create empirical mappings from molecular dynamic simulation to assist interpreting these IR spectra, but often use a limited set of model systems to parameterize their map. Here, we reveal a creation of a library of di- and tri-peptides that are prevalently present in biological systems. This library of IR spectra can be used to validate current empirical mappings and be a resource for improving current models.

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