Journal
MACROMOLECULES
Volume 51, Issue 3, Pages 1058-1068Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.macromol.7b02627
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Funding
- Ministry of Education, Science, Culture and Supports of Japan [JP26248050]
- Impulsing Paradigm Change through Disruptive Technologies Program (ImPACT)
- Grants-in-Aid for Scientific Research [26248050] Funding Source: KAKEN
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For the first time, we determined the relative percentages of rectangular and staggered packing arrangements in the crystalline polyalanine regions with antiparallel beta-sheet structure within spider dragline silk fiber from Nephila clavata (NCF) and recombinant silk protein (RSP). The methods used included X-ray diffraction and C-13 NMR coupled with selective C-13 isotope labeling of the Ala C beta carbons. From deconvolution analyses of the Ala C beta peaks in the C-13 CP/MAS NMR spectra, the relative percentages of the rectangular arrangements in [3-C-13]AlaNCF were determined to be 49 +/- 8% and 40 +/- 7% in the dry and hydrated states, respectively, and in [3-C-13]Ala-RSP 62 +/- 11% and 81 +/- 5% in the dry and hydrated states, respectively. Thus, the packing structure changed significantly between the two spider silks and also between the two physical states. The use of NMR was critical in this analysis; from X-ray diffraction patterns alone it would have been difficult to obtain these quantitative data.
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