Toward high-resolution computational design of the structure and function of helical membrane proteins

Nat Struct Mol Biol. 2016 Jun 7;23(6):475-80. doi: 10.1038/nsmb.3231.

Abstract

The computational design of α-helical membrane proteins is still in its infancy but has already made great progress. De novo design allows stable, specific and active minimal oligomeric systems to be obtained. Computational reengineering can improve the stability and function of naturally occurring membrane proteins. Currently, the major hurdle for the field is the experimental characterization of the designs. The emergence of new structural methods for membrane proteins will accelerate progress.

MeSH terms

  • Calcium-Transporting ATPases / chemistry*
  • Computer-Aided Design*
  • Escherichia coli / chemistry
  • Escherichia coli Proteins / chemistry*
  • Humans
  • Models, Molecular
  • Monosaccharide Transport Proteins / chemistry*
  • Protein Engineering*
  • Protein Stability
  • Protein Structure, Secondary
  • Research Design
  • Symporters / chemistry*
  • Thermodynamics

Substances

  • Escherichia coli Proteins
  • LacY protein, E coli
  • Monosaccharide Transport Proteins
  • Symporters
  • Calcium-Transporting ATPases