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Raman Spectroscopic Evidence for Side-Chain Unfolding in Spider Dragline Silk under Tensile Deformation

Published online by Cambridge University Press:  01 February 2011

Xiaojun He
Affiliation:
School of Materials Science & Engineering, 161 Sirrine Hall
Michael S. Ellison
Affiliation:
School of Materials Science & Engineering, 161 Sirrine Hall
Jacqueline M. Palmer
Affiliation:
Department of Genetics, Biochemistry & Life Science Studies; Clemson University, Clemson, South Carolina 29634-0971
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Abstract

In-situ Ramanspectra were collected on the N. clavipes spider dragline silk under a tensile deformation rate of 15mm/min. The most prominent features on the spectra were due to those bands near 1100 cm-1, which present as a sensitive probe to structural changes associated with side-chains of silk peptide. A downshift of Raman bands at 1095 cm-1 and 1089 cm-1 was detected with increasing strain. Furthermore, an increase in the intensity of the Raman band at 1062 cm-1 due to the vibration of trans structure without lateral coupling was prominent at certain strain levels. This was interpreted in terms of a morphology transition from the random configuration to the trans conformation modulated by the reorganization of the hydrogen bonding among the side-chain.

Type
Research Article
Copyright
Copyright © Materials Research Society 2005

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References

1. Sirichaisit, J., Young, R. J., Vollrath, F., Polym. 41, 12231227 (2000).Google Scholar
2. Sirichaisit, J., Brookes, V. L., Young, R. J., Vollrath, F., Biomacromolecules 4, 387394 (2003).Google Scholar
3. Gillespie, B. D., Viney, C., Yager, P., In Silk Polymers, Materials Science and Biotechnology, Kaplan, D. L., Adams, W., Farmer, B., Viney, C., Eds.; American Chemical Society: Washington, DC, 1994; Chapter 14, p 155.Google Scholar
4. Thomas, G. J. Jr, Prescott, B., J. Mol. Biol. 165, 321356(1983).Google Scholar
5. Vogel, H., Jähnig, F., Chemistry and Physics of Lipids 29, 83101 (1981).Google Scholar
6. Krimm, S., Bandekar, J., Advances in Protein Chemistry, 38, 183364 (1982).Google Scholar
7. Faiman, R., Chemistry and Physics of Lipids 23, 7784 (1979).Google Scholar
8. Chou, J. J., Case, D. A., Bax, A. D., J. Am. Chem. Soc. 123, 89598966 (2003).Google Scholar
9. Janin, J., Wodak, S. J. Mol. Biol. 125, 357386 (1978).Google Scholar
10. Shao, Z., Vollrath, F., Sirichaisit, J., Young, R. J., Polym. 40, 24932500 (1999).Google Scholar
11. He, X., Ellison, M. S., Palmer, J. M. “Conformational study of dragline silk under controlled supercontraction” in preparation.Google Scholar
12. Edwards, H., Farwell, D. W., J. Raman Spectroscopy 26, 901909(1995).Google Scholar