期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 56, 期 41, 页码 12571-12575出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201706649
关键词
biomimicry; fibrous proteins; NMR spectroscopy; spider silk
资金
- EC [316149]
- Swedish Research Council
- Center for Innovative Medicine (CIMED) at Karolinska Institutet
- Stockholm City Council
Biomimetic spinning of artificial spider silk requires that the terminal domains of designed minispidroins undergo specific structural changes in concert with the beta-sheet conversion of the repetitive region. Herein, we combine solution and solid-state NMR methods to probe domain-specific structural changes in the NT2RepCT minispidroin, which allows us to assess the degree of biomimicry of artificial silk spinning. In addition, we show that the structural effects of post-spinning procedures can be examined. By studying the impact of NT2RepCT fiber drying, we observed a reversible beta-to-alpha conversion. We think that this approach will be useful for guiding the optimization of artificial spider silk fibers.
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