Viscoelastic relaxation time and structural evolution during length contraction of spider silk protein nanostructures

Graham Bratzel, Zhao Qin, Markus J. Buehler

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)185-190
Number of pages6
JournalMRS Communications
Volume3
Issue number3
DOIs
StatePublished - Jan 1 2013
Externally publishedYes

ASJC Scopus subject areas

  • Materials Science(all)

Fingerprint Dive into the research topics of 'Viscoelastic relaxation time and structural evolution during length contraction of spider silk protein nanostructures'. Together they form a unique fingerprint.

  • Cite this