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• W2746340333 abstract "Spider dragline silk is a protein material that has evolved over millions of years to achieve finely tuned mechanical properties. A less known feature of some dragline silk fibers is that they shrink along the main axis by up to 50% when exposed to high humidity, a phenomenon called supercontraction. This contrasts the typical behavior of many other materials that swell when exposed to humidity. Molecular level details and mechanisms of the supercontraction effect are heavily debated. Here we report a molecular dynamics analysis of supercontraction in Nephila clavipes silk combined with in situ mechanical testing and Raman spectroscopy linking the reorganization of the nanostructure to the polar and charged amino acids in the sequence. We further show in our in silico approach that point mutations of these groups not only suppress the supercontraction effect, but even reverse it, while maintaining the exceptional mechanical properties of the silk material. This work has imminent impact on the design of biomimetic equivalents and recombinant silks for which supercontraction may or may not be a desirable feature. The approach applied is appropriate to explore the effect of point mutations on the overall physical properties of protein based materials." @default.
• W2746340333 created "2017-08-31" @default.
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• W2746340333 date "2017-09-19" @default.
• W2746340333 modified "2023-10-10" @default.
• W2746340333 title "Unraveling the Molecular Requirements for Macroscopic Silk Supercontraction" @default.
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• W2746340333 doi "https://doi.org/10.1021/acsnano.7b01532" @default.
• W2746340333 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28846384" @default.
• W2746340333 hasPublicationYear "2017" @default.
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