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PMID: 8539605 Published · ppublish English Comment Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk.

Science (New York, N.Y.) ·Vol. 271 ·No. 5245 ·1996-01-05 ·Pages 84-7

Simmons AH, Michal CA, Jelinski LW

Abstract

The molecular origin of the exceptional mechanical properties of spider silk is unclear. This paper presents solid-state 2H nuclear magnetic resonance data from unoriented, oriented, and supercontracted fibers, indicating that the crystalline fraction of dragline silk consists of two types of alanine-rich regions, one that is highly oriented and one that is poorly oriented and less densely packed. A new model for the molecular-level structure of individual silk molecules and their arrangement in the fibers is proposed. These data suggest that it will be necessary to control the secondary structure of individual polymer molecules in order to obtain optimum properties in bio-inspired polymers.

MeSH Terms
Alanine/analysis Algorithms Amino Acid Sequence Animals Crystallization Crystallography, X-Ray Fibroins Glycine/analysis Insect Proteins Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptides/analysis Protein Conformation Protein Structure, Secondary Proteins/chemistry Silk Spiders/chemistry
Chemicals
Insect Proteins Peptides Proteins Silk spidroin 2 polyalanine Fibroins Alanine Glycine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Simmons A H
Center for Advanced Technology in Biotechnology, Cornell University, Ithaca, NY 14853, USA.
Michal C A
Jelinski L W
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1996-01-05
Pages
84-7
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Corrections
CommentOn
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