Orientation, structure, wet-spinning, and molecular basis for supercontraction of spider dragline silk
1999; Elsevier BV; Volume: 24; Issue: 2-3 Linguagem: Inglês
10.1016/s0141-8130(98)00085-3
ISSN1879-0003
AutoresLynn W. Jelinski, Amy Blye, Oskar Liivak, Carl A. Michal, George LaVerde, Andreas Seidel, Neeral Shah, Zhitong Yang,
Tópico(s)Invertebrate Immune Response Mechanisms
ResumoThis 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.
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