NMR characterization of native liquid spider dragline silk from Nephila edulis
NMR characterization of native liquid spider dragline silk from Nephila edulis
Solid spider dragline silk is well-known for its mechanical properties. Nonetheless a detailed picture of the spinning process is lacking. Here we report NMR studies on the liquid silk within the wide sac of the major ampullate (m.a.) gland from the spider Nephila edulis. The resolution in the NMR spectra is shown to be significantly improved by the application of magic-angle spinning (MAS). From the narrow width of the resonance lines and the chemical shifts observed, it is concluded that the silk protein within the wide sac of the m.a. gland is dynamically disordered throughout the molecule in the sense that each amino acid of a given type senses an identical environment, on average. The NMR data obtained are consistent with an isotropic liquid phase.
834-839
Hronska, M.
8a042c0c-362e-4500-8955-a15797d52d93
van Beek, J.D.
24c54019-2538-42d7-9740-18d1ce13c7f2
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Vollrath, Fritz
bae608b8-81dc-4471-96fb-5d0aca9363d2
Meier, Beat H.
f0c14a56-63f1-4e30-9af7-6d51064ed1df
May 2004
Hronska, M.
8a042c0c-362e-4500-8955-a15797d52d93
van Beek, J.D.
24c54019-2538-42d7-9740-18d1ce13c7f2
Williamson, P.T.F.
0b7715c6-b60e-4e95-a1b1-6afc8b9f372a
Vollrath, Fritz
bae608b8-81dc-4471-96fb-5d0aca9363d2
Meier, Beat H.
f0c14a56-63f1-4e30-9af7-6d51064ed1df
Hronska, M., van Beek, J.D., Williamson, P.T.F., Vollrath, Fritz and Meier, Beat H.
(2004)
NMR characterization of native liquid spider dragline silk from Nephila edulis.
Biomacromolecules, 5 (3), .
(doi:10.1021/bm0343904).
Abstract
Solid spider dragline silk is well-known for its mechanical properties. Nonetheless a detailed picture of the spinning process is lacking. Here we report NMR studies on the liquid silk within the wide sac of the major ampullate (m.a.) gland from the spider Nephila edulis. The resolution in the NMR spectra is shown to be significantly improved by the application of magic-angle spinning (MAS). From the narrow width of the resonance lines and the chemical shifts observed, it is concluded that the silk protein within the wide sac of the m.a. gland is dynamically disordered throughout the molecule in the sense that each amino acid of a given type senses an identical environment, on average. The NMR data obtained are consistent with an isotropic liquid phase.
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Published date: May 2004
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Local EPrints ID: 56445
URI: http://eprints.soton.ac.uk/id/eprint/56445
ISSN: 1525-7797
PURE UUID: 5f73dd2b-ef17-453d-bd1f-bae8df7a5b97
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Date deposited: 07 Aug 2008
Last modified: 16 Mar 2024 03:53
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Contributors
Author:
M. Hronska
Author:
J.D. van Beek
Author:
Fritz Vollrath
Author:
Beat H. Meier
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