Date of Award
1-1-2013
Language
English
Document Type
Dissertation
Degree Name
Doctor of Philosophy (PhD)
College/School/Department
Department of Chemistry
Content Description
1 online resource (xi, 146 pages) : illustrations (some color)
Dissertation/Thesis Chair
Alexander Shekhtman
Committee Members
Jayanti Pande, Carla Theimer, Kathleen McDonough, Igor Lednev
Keywords
amyloid fibrils, intrinsically disordered proteins, Amyloid, Amyloid beta-protein, Proteins
Subject Categories
Biochemistry
Abstract
Amyloid fibrils are β-sheet-rich protein aggregates commonly found in the organs and tissues of patients with various amyloid-associated diseases. The structure of insulin fibrils was characterized by deep ultraviolet resonance Raman and Nuclear Magnetic Resonance spectroscopy combined with hydrogen-deuterium exchange. Our new approach of combining NMR and Raman spectroscopy with molecular dynamic simulations for characterizing amyloid fibrils provided exclusive knowledge about fibril structure at amino acid residue resolution.
Recommended Citation
Washington, Jacqueline D., "New tools to study amyloid fibrils and intrinsically disordered proteins in vitro and in vivo" (2013). Legacy Theses & Dissertations (2009 - 2024). 1040.
https://scholarsarchive.library.albany.edu/legacy-etd/1040