Designing supramolecular protein assemblies

Curr Opin Struct Biol. 2002 Aug;12(4):464-70. doi: 10.1016/s0959-440x(02)00350-0.

Abstract

Many natural proteins self-assemble, either to fulfill their biological function or as part of a pathogenic process. Biological assembly phenomena such as amyloidogenesis, domain swapping and symmetric oligomerization are inspiring new strategies for designing proteins that self-assemble to form supramolecular complexes. Recent advances include the design of novel proteins that assemble into filaments, symmetric cages and regular arrays.

Publication types

  • Review

MeSH terms

  • Amyloid / chemistry
  • Macromolecular Substances*
  • Models, Molecular
  • Nanotechnology*
  • Protein Conformation*
  • Protein Engineering / methods*
  • Protein Engineering / trends
  • Protein Folding*
  • Protein Structure, Secondary
  • Proteins / chemistry*

Substances

  • Amyloid
  • Macromolecular Substances
  • Proteins