Quantifying the fraction of glycine and alanine in β-sheet and helical conformations in spider dragline silk using solid-state NMR
文献信息
Gregory P. Holland, Janelle E. Jenkins, Melinda S. Creager, Randolph V. Lewis, Jeffery L. Yarger
Solid-state two-dimensional refocused INADEQUATE MAS NMR experiments resolve distinct helical and β-sheet conformational environments for both alanine and glycine in Nephila clavipes dragline silk fibers; the fraction of alanine and glycine in β-sheet structures is determined to be 82% ± 4% and 28% ± 5%, respectively.
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Chemical Communications

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry














