Journal
BIOMACROMOLECULES
Volume 18, Issue 1, Pages 231-241Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biomac.6b01537
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Spider major ampullate silk is often schematically represented as a two-phase material composed of crystalline nanodomains in an amorphous matrix. Here we are interested in revealing its more complex nanoscale organization by probing Argiope bruennichi dragline-type fibers using scanning X-ray nanodiffraction. This allows resolving transversal structural features such as an about 1 pm skin layer composed of around 100 nm diameter nanofibrils serving presumably as an elastic sheath. The core consists of a composite of several nm size crystalline nanodomains with poly(L-alanine) microstructure, embedded in a polypeptide network with Short-range order. Stacks of nanodomains separated by less ordered nanosegments form nanofibrils with a periodic axial density modulation which is particularly sensitive to radiation damage. The precipitation of larger beta-type nanocrystallites in the outer core shell is attributed to MaSp1 protein molecules.
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