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Int J Biol Macromol. 1999 Mar-Apr;24(2-3):197-201.

Orientation, structure, wet-spinning, and molecular basis for supercontraction of spider dragline silk.

Author information

1
Center for Advanced Technology in Biotechnology, Cornell University, Ithaca, NY 14853, USA.

Abstract

This manuscript reviews work from our laboratory that addresses the orientation, secondary structure, wet-spinning, and molecular basis for supercontraction of spider silk. It identifies the poly(alanine) runs as the crystalline regions, establishes the degree of orientation of these regions, and identifies the secondary structural elements of the conserved L-G-X-Q (X = G, S, or N) regions. It also describes methods for spinning very small amounts of protein polymers and it sets forth several molecular-level hypotheses concerning supercontraction.

PMID:
10342765
DOI:
10.1016/s0141-8130(98)00085-3
[Indexed for MEDLINE]

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