Quantifying the fraction of glycine and alanine in beta-sheet and helical conformations in spider dragline silk using solid-state NMR.
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.
Holland
Gregory P
GP
Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA. greg.holland@asu.edu
Jenkins
Janelle E
JE
Creager
Melinda S
MS
Lewis
Randolph V
RV
Yarger
Jeffery L
JL
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
D002247:Carbon Isotopes; D047011:Silk; D000409:Alanine; D005998:Glycine