Spider dragline silk is a self-assembling protein that rivals many engineering fibers in strength, extensibility, and toughness, making it a versatile biocompatible material. Here, atomistic-level structures of wildtype MaSp1 protein from the Nephila clavipes spider dragline silk sequences, obtained using an in silico approach based on replica exchange molecular dynamics and explicit water, are subjected to nanomechanical testing and released preceding failure. We approximate the relaxation time from an exponential decay function, and identify permanent changes in secondary structure. Our work provides fundamental insights into the time-dependent properties of silk and possibly other protein materials.
|Original language||English (US)|
|Number of pages||6|
|State||Published - 2013|
ASJC Scopus subject areas
- Materials Science(all)