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Conformational Energy Studies of Model Silk Fibroin Peptides

Published online by Cambridge University Press:  15 February 2011

Stephen A. Fossey
Affiliation:
On leave from US Army Natick Research, Development and Engineering Center, Natick, Massachusetts 01760–5020
G. Nemethy
Affiliation:
Baker Laboratory of Chemistry, Cornell University, Ithaca, New York 14853–1301.
K. D. Gibson
Affiliation:
Baker Laboratory of Chemistry, Cornell University, Ithaca, New York 14853–1301.
H. A. Scheraga
Affiliation:
Baker Laboratory of Chemistry, Cornell University, Ithaca, New York 14853–1301.
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Extract

Silk-like proteins are a topic of long-standing scientific interest and recently are being considered for such uses as high performance fibers [1] and enzyme-immobilizing substrates [2]. The structure of silk (in particular, the metastable silk I form) is critical in understanding the formation and processing of these materials.

Computations provide a useful tool for the detailed modeling of the structures of fibrous proteins. Conformational energy calculations on representative model polypeptides have been used successfully to elucidate the structure of collagen [3]. We have applied this method to the study of the crystalline region of Bombvx mori silk fibroin [4].

Type
Research Article
Copyright
Copyright © Materials Research Society 1991

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References

1. Lombardi, S. J., Fossey, S. A., and Kaplan, D. L.; Proceedings of the American Society for Composites - Fifth Technical Conference, June 1990.Google Scholar
2. Demura, M. and Asakura, T. (1989) Biotech. and Bioeng. 33, 598603.Google Scholar
3. Nemethy, G. and Scheraga, H. A. (1989) Bull. Inst. Chem. Res. Univ. Kyoto 66, 398408.Google Scholar
4. Fossey, S. A., Nemethy, G., Gibson, K. D., and Scheraga, H. A.. Manuscript in preparation.Google Scholar
5. Fraser, R. B. D. and MacRae, T. P. (1973) In “Conformation of Fibrous Proteins and Related Synthetic Polypeptides”; p312 Academic Press New York. Google Scholar
6. Lotz, B. and Keith, H. D. (1971) J. Mol. Biol. 61, 201215.CrossRefGoogle Scholar