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Elucidating the Molecular Dynamics, Structure and Assembly of Spider Dragline Silk Proteins by Nuclear Magnetic Resonance (NMR) Spectroscopy


Abstract Spider dragline silk is an outstanding biopolymer with a strength that exceeds steel by weight and a toughness greater than high-performance fibers like Kevlar. For this reason, structural and dynamic studies on the spider silk are of great importance for developing future biomaterials. The spider dragline silk comprises two silk proteins, Major ampullate Spidroin 1 and 2 (MaSp1 and 2), which are synthesized and stored in the major ampullate (MA) gland of spiders. The initial state of the silk proteins within Black Widow MA glands was probed with solution-state NMR spectroscopy. The conformation dependent chemical shifts information indicates that the silk proteins are unstructured and in random coil conformation. 15N relaxation parameters,... (more)
Created Date 2015
Contributor Xu, Dian (Author) / Yarger, Jeffery L (Advisor) / Holland, Gregory P (Advisor) / Wang, Xu (Committee member) / Liu, Yan (Committee member) / Arizona State University (Publisher)
Subject Chemistry / Biophysics / Analytical chemistry / Intrinsic Disordered Protein / NMR / Protein Dynamics / Protein Structure / Self Assembly / Spider Silk
Type Doctoral Dissertation
Extent 177 pages
Language English
Copyright
Reuse Permissions All Rights Reserved
Note Doctoral Dissertation Chemistry 2015
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


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Description Dissertation/Thesis