Protein stabilization in a highly knotted protein polymer

Protein Eng Des Sel. 2011 Aug;24(8):627-30. doi: 10.1093/protein/gzr024. Epub 2011 Jun 13.

Abstract

The polypeptide backbones of a few proteins are tied in a knot. The biophysical effects and potential biological roles of knots are not well understood. Here, we test the consequences of protein knotting by taking a monomeric protein, carbonic anhydrase II, whose native structure contains a shallow knot, and polymerizing it end-to-end to form a deeply and multiply knotted polymeric filament. Thermal stability experiments show that the polymer is stabilized against loss of structure and aggregation by the presence of deep knots.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Carbonic Anhydrase II / chemistry*
  • Chromatography, Gel
  • Disulfides / chemistry
  • Humans
  • Models, Molecular
  • Polymerization
  • Protein Conformation
  • Protein Stability
  • Temperature

Substances

  • Disulfides
  • Carbonic Anhydrase II