Controlling the structure of proteins at surfaces

J Am Chem Soc. 2010 Dec 8;132(48):17277-81. doi: 10.1021/ja107212z. Epub 2010 Nov 16.

Abstract

With the help of single molecule force spectroscopy and molecular dynamics simulations, we determine the surface-induced structure of a single engineered spider silk protein. An amyloid like structure is induced in the vicinity of a surface with high surface energy and can be prohibited in the presence of a hydrophobic surface. The derived molecular energy landscapes highlight the role of single silk protein structure for the macroscopic toughness of spider silk.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fibroins / chemistry*
  • Microscopy, Atomic Force
  • Molecular Dynamics Simulation
  • Peptide Fragments / chemistry
  • Protein Structure, Secondary
  • Surface Properties
  • Thermodynamics

Substances

  • Peptide Fragments
  • Fibroins