Membrane proteins: from bench to bits

Biochem Soc Trans. 2011 Jun;39(3):747-50. doi: 10.1042/BST0390747.

Abstract

Membrane proteins currently receive a lot of attention, in large part thanks to a steady stream of high-resolution X-ray structures. Although the first few structures showed proteins composed of tightly packed bundles of very hydrophobic more or less straight transmembrane α-helices, we now know that helix-bundle membrane proteins can be both highly flexible and contain transmembrane segments that are neither very hydrophobic nor necessarily helical throughout their lengths. This raises questions regarding how membrane proteins are inserted into the membrane and fold in vivo, and also complicates life for bioinformaticians trying to predict membrane protein topology and structure.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Crystallography, X-Ray
  • Hydrophobic and Hydrophilic Interactions
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary*
  • Protein Structure, Tertiary*

Substances

  • Membrane Proteins