Document Type
Article
Publication Date
12-2-2016
Keywords
Amino Acid Sequence, Animals, Fibroins, Molecular Dynamics Simulation, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Repetitive Sequences, Amino Acid
Digital Object Identifier (DOI)
https://doi.org/10.3390/ijms17122023
Abstract
Solid-state NMR and molecular dynamics (MD) simulations are presented to help elucidate the molecular secondary structure of poly(Gly-Gly-X), which is one of the most common structural repetitive motifs found in orb-weaving dragline spider silk proteins. The combination of NMR and computational experiments provides insight into the molecular secondary structure of poly(Gly-Gly-X) segments and provides further support that these regions are disordered and primarily non-β-sheet. Furthermore, the combination of NMR and MD simulations illustrate the possibility for several secondary structural elements in the poly(Gly-Gly-X) regions of dragline silks, including β-turns, 3
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
International Journal of Molecular Sciences, v. 17, issue 12, art. 2023
Scholar Commons Citation
Gray, Geoffrey M; van der Vaart, Arjan; Guo, Chengchen; Jones, Justin; Onofrei, David; Cherry, Brian R; Lewis, Randolph V; Yarger, Jeffery L; and Holland, Gregory P, "Secondary Structure Adopted by the Gly-Gly-X Repetitive Regions of Dragline Spider Silk" (2016). Chemistry Faculty Publications. 16.
https://digitalcommons.usf.edu/chm_facpub/16
