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The structure of a single thread of Nephila edulis silk has been studied by in situ X-ray diffraction from a living spider. A systematic increase of orientational order with increasing silking speed up to 40 mm s-1 was observed. Within a few mm from the spinnerets exit, crystalline domains with a beta-poly(L-alanine) structure were observed. The data also suggest an increase in crystalline fraction in the immediate vicinity of the spigot exit.

Original publication

DOI

10.1021/bm000047c

Type

Journal article

Journal

Biomacromolecules

Publication Date

2000

Volume

1

Pages

622 - 626

Keywords

Algorithms, Animals, Crystallography, X-Ray, Insect Proteins, Microscopy, Electron, Scanning, Silk, Spiders, Synchrotrons, Tensile Strength, X-Rays