Theses and Dissertations

Yue Zhang

Issuing Body

Mississippi State University

Advisor

Fitzkee, Nicholas C.

Committee Member

Lewis, Edwin A.

Committee Member

Emerson, Joseph P.

Date of Degree

5-17-2014

Original embargo terms

MSU Only Indefinitely

Document Type

Graduate Thesis - Campus Access Only

Major

Chemistry

Degree Name

Master of Science

College

College of Arts and Sciences

Department

Department of Chemistry

Abstract

The random-coil model has been dominant for unfolded proteins since the 1950’s; however, some experiments showed that the unfolded proteins were biased toward specific conformations in conflict with the random-coil model. Recently, residual dipolar couplings (RDCs) and paramagnetic relaxation enhancement (PRE) were applied to obtain a large amount of structural information on unfolded proteins. Typically, these data were interpreted in a framework of random-coil ensembles with a good agreement between experimental data and theoretical predictions. In this thesis, it was tested whether locally organized nonrandom ensembles could describe this agreement equally as well. Using a complete set of RDC and PRE data for denatured ubiquitin, it was revealed that there was no distinguishable difference between random-coil ensembles and ensembles containing 50% native structure. Thus, while it is important to measure as many RDCs or PRE as possible, even the best datasets may be insensitive to local organization in unfolded proteins.

URI

https://hdl.handle.net/11668/19249

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