title: Secondary Structure Adopted by the Gly-Gly-X Repetitive Regions of Dragline Spider Silk.
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, 310-helicies, and coil structures with a negligible population of α-helix observed.
authors.affiliation: Department of Chemistry, University of South Florida, 4202 East Fowler Avenue CHE 205, Tampa, FL 33620-9998, USA. gmgray2@mail.usf.edu.
authors.forename: Geoffrey M
authors.initials: GM
authors.lastname: Gray
authors.affiliation: Department of Chemistry, University of South Florida, 4202 East Fowler Avenue CHE 205, Tampa, FL 33620-9998, USA. avandervaart@usf.edu.
authors.forename: Arjan
authors.initials: A
authors.lastname: van der Vaart
authors.affiliation: School of Molecular Sciences and the Magnetic Resonance Research Center, Arizona State University, Tempe, AZ 85287-1604, USA. daniel_guo1226@hotmail.com.
authors.forename: Chengchen
authors.initials: C
authors.lastname: Guo
authors.affiliation: Department of Biology and Synthetic Biomanufacturing Center, Utah State University, 650 East 1600 North, North Logan, UT 84341, USA. justin.a.jones@usu.edu.
authors.forename: Justin
authors.initials: J
authors.lastname: Jones
authors.affiliation: Department of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182-1030, USA. romanianknight@gmail.com.
authors.forename: David
authors.initials: D
authors.lastname: Onofrei
authors.affiliation: School of Molecular Sciences and the Magnetic Resonance Research Center, Arizona State University, Tempe, AZ 85287-1604, USA. brian.r.cherry@asu.edu.
authors.forename: Brian R
authors.initials: BR
authors.lastname: Cherry
authors.affiliation: Department of Biology and Synthetic Biomanufacturing Center, Utah State University, 650 East 1600 North, North Logan, UT 84341, USA. randy.lewis@usu.edu.
authors.forename: Randolph V
authors.initials: RV
authors.lastname: Lewis
authors.affiliation: School of Molecular Sciences and the Magnetic Resonance Research Center, Arizona State University, Tempe, AZ 85287-1604, USA. jyarger@gmail.com.
authors.forename: Jeffery L
authors.initials: JL
authors.lastname: Yarger
authors.affiliation: Department of Chemistry and Biochemistry, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182-1030, USA. gholland@mail.sdsu.edu.
authors.forename: Gregory P
authors.initials: GP
authors.lastname: Holland
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005349:Fibroins / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D020449:Repetitive Sequences, Amino Acid
chemical_list: C076815:spidroin 2; D005349:Fibroins
keywords: NMR; molecular dynamics; secondary structure; solid-state NMR; spider silk