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

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Creative Commons License
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

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Chemistry Commons

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