title: Quantifying the fraction of glycine and alanine in beta-sheet and helical conformations in spider dragline silk using solid-state NMR.
abstract: Solid-state two-dimensional refocused INADEQUATE MAS NMR experiments resolve distinct helical and beta-sheet conformational environments for both alanine and glycine in Nephila clavipes dragline silk fibers; the fraction of alanine and glycine in beta-sheet structures is determined to be 82% +/- 4% and 28% +/- 5%, respectively.
authors.affiliation: Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA. greg.holland@asu.edu
authors.forename: Gregory P
authors.initials: GP
authors.lastname: Holland
authors.forename: Janelle E
authors.initials: JE
authors.lastname: Jenkins
authors.forename: Melinda S
authors.initials: MS
authors.lastname: Creager
authors.forename: Randolph V
authors.initials: RV
authors.lastname: Lewis
authors.forename: Jeffery L
authors.initials: JL
authors.lastname: Yarger
mesh_terms: D000409:Alanine / Q000737:chemistry*; D000818:Animals; D002247:Carbon Isotopes; D005998:Glycine / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods* / Q000592:standards; D017433:Protein Structure, Secondary; D012015:Reference Standards; D047011:Silk / Q000737:chemistry*; D013112:Spiders
chemical_list: D002247:Carbon Isotopes; D047011:Silk; D000409:Alanine; D005998:Glycine