Investigating protein folding through EPR spectroscopy

Date of Award




Document Type

Master's Thesis

Degree Name

Master of Science (MS)


Department of Chemistry

Content Description

1 online resource (xi, 90 pages) : illustrations (some color)

Dissertation/Thesis Chair

Carla Theimer


Electron Paramagnetic Resonance, EPR, Protein-Folding, Protein folding, Electron paramagnetic resonance spectroscopy, Proteins

Subject Categories

Biochemistry | Biophysics | Chemistry


In the 1970's, Noble Laureate Christian Anfinsen and colleagues hypothesized that a protein's native structure did not depend upon how it was folded into that structure (what process), but which structure was the most thermodynamically stable conformation. This led to the Levinthal Paradox. The Levinthal paradox is a concept that attempts to explain a folding mechanism that allows a protein to search its conformational space quickly in order to find the most stable conformation (usually the lowest in free energy). Investigation of the protein folding question is critical to understanding protein misfolding diseases like Creutzfeldt-Jakob disease, Alzheimer's, Parkinson's and Huntington's diseases.

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