Investigating protein folding through EPR spectroscopy
Date of Award
1-1-2014
Language
English
Document Type
Master's Thesis
Degree Name
Master of Science (MS)
College/School/Department
Department of Chemistry
Content Description
1 online resource (xi, 90 pages) : illustrations (some color)
Dissertation/Thesis Chair
Carla Theimer
Keywords
Electron Paramagnetic Resonance, EPR, Protein-Folding, Protein folding, Electron paramagnetic resonance spectroscopy, Proteins
Subject Categories
Biochemistry | Biophysics | Chemistry
Abstract
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.
Recommended Citation
Antonucci, Anneliese, "Investigating protein folding through EPR spectroscopy" (2014). Legacy Theses & Dissertations (2009 - 2024). 1067.
https://scholarsarchive.library.albany.edu/legacy-etd/1067