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  4. Molecular structure and dynamics of spider silk and venom proteins investigated by nuclear magnetic resonance
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Molecular structure and dynamics of spider silk and venom proteins investigated by nuclear magnetic resonance

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Description

Spider dragline silk is well known for its outstanding mechanical properties - a combination of strength and extensibility that makes it one of the toughest materials known. Two proteins, major ampullate spidroin 1 (MaSp1) and 2 (MaSp2), comprise dragline silk fibers. There has been considerable focus placed on understanding the source of spider silk's unique mechanical properties by investigating the protein composition, molecular structure and dynamics. Chemical compositional heterogeneity of spider silk fiber is critical to understand as it provides important information for the interactions between MaSp1 and MaSp2. Here, the amino acid composition of dragline silk protein was precisely determined using a solution-state nuclear magnetic resonance (NMR) approach on hydrolyzed silk fibers. In a similar fashion, solution-state NMR was applied to probe the "13"C/"15"N incorporation in silk, which is essential to understand for designing particular solid-state NMR methods for silk structural characterization. Solid-state NMR was used to elucidate silk protein molecular dynamics and the supercontraction mechanism. A "2"H-"13"C heteronuclear correlation (HETCOR) solid-state NMR technique was developed to extract site-specific "2"H quadrupole patterns and spin-lattice relaxation rates for understanding backbone and side-chain dynamics. Using this technique, molecular dynamics were determined for a number of repetitive motifs in silk proteins - Ala residing nanocrystalline &beta-sheet; domains, 3"1"-helical regions, and, Gly-Pro-Gly-XX &beta-turn; motifs. The protein backbone and side-chain dynamics of silk fibers in both dry and wet states reveal the impact of water on motifs with different secondary structures. Spider venom is comprised of a diverse range of molecules including salts, small organics, acylpolyamines, peptides and proteins. Neurotoxins are an important family of peptides in spider venom and have been shown to target and modulate various ion channels. The neurotoxins are Cys-rich and share an inhibitor Cys knot (ICK) fold. Here, the molecular structure of one G. rosea tarantula neurotoxin, GsAF2, was determined by solution-state NMR. In addition, the interaction between neurotoxins and model lipid bilayers was probed with solid-state NMR and negative-staining (NS) transmission electron microscopy (TEM). It is shown that the neurotoxins influence lipid bilayer assembly and morphology with the formation of nanodiscs, worm-like micelles and small vesicles.

Date Created
2014
Contributors
  • Shi, Xiangyan (Author)
  • Yarger, Jeffery L (Thesis advisor)
  • Holland, Gregory P (Thesis advisor)
  • Levitus, Marcia (Committee member)
  • Marzke, Robert F (Committee member)
  • Arizona State University (Publisher)
Topical Subject
  • Biophysics
  • Biochemistry
  • Physical Chemistry
  • Molecular Dynamics
  • Molecular structure
  • NMR
  • Spider Silk
  • Spider Venom Proteins
  • Spider webs--Analysis.
  • Spider webs
  • Poisonous spiders--Venom--Analysis.
  • Poisonous spiders
  • Proteins--Analysis.
Resource Type
Text
Genre
Doctoral Dissertation
Academic theses
Extent
xv, 236 p. : ill. (some col.)
Language
eng
Copyright Statement
In Copyright
Reuse Permissions
All Rights Reserved
Primary Member of
ASU Electronic Theses and Dissertations
Peer-reviewed
No
Open Access
No
Handle
https://hdl.handle.net/2286/R.I.24897
Embargo Release Date
Sat, 04/30/2016 - 21:28
Statement of Responsibility
by Xiangyan Shi
Description Source
Retrieved on July 15, 2014
Level of coding
full
Note
Partial requirement for: Ph.D., Arizona State University, 2014
Note type
thesis
Includes bibliographical references
Note type
bibliography
Field of study: Chemistry
System Created
  • 2014-06-09 02:09:26
System Modified
  • 2021-08-30 01:35:27
  •     
  • 1 year 6 months ago
Additional Formats
  • OAI Dublin Core
  • MODS XML

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