English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Degree of biomimicry of artificial spider silk spinning assessed by NMR spectroscopy.

MPS-Authors
/persons/resource/persons206080

Andreas,  L. B.
Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)

2502796_Suppl.pdf
(Supplementary material), 2MB

Citation

Otikovs, M., Andersson, M., Jia, Q., Nordling, K., Meng, Q., Andreas, L. B., et al. (2017). Degree of biomimicry of artificial spider silk spinning assessed by NMR spectroscopy. Angewandte Chemie International Edition, 56(41), 12571-12575. doi:10.1002/anie.201706649.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-2EC2-0
Abstract
Biomimetic spinning of artificial spider silk requires that the terminal domains of designed minispidroins undergo specific structural changes in concert with the β-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.