Structure and function of proteins in membranes and nanodiscs

Biochim Biophys Acta Biomembr. 2021 Jan 1;1863(1):183445. doi: 10.1016/j.bbamem.2020.183445. Epub 2020 Aug 22.

Abstract

The field of membrane structural biology represents a fast-moving field with exciting developments including native nanodiscs that allow preparation of complexes of post-translationally modified proteins bound to biological lipids. This has led to conceptual advances including biological membrane:protein assemblies or "memteins" as the fundamental functional units of biological membranes. Tools including cryo-electron microscopy and X-ray crystallography are maturing such that it is becoming increasingly feasible to solve structures of large, multicomponent complexes, while complementary methods including nuclear magnetic resonance spectroscopy yield unique insights into interactions and dynamics. Challenges remain, including elucidating exactly how lipids and ligands are recognized at atomic resolution and transduce signals across asymmetric bilayers. In this special volume some of the latest thinking and methods are gathered through the analysis of a range of transmembrane targets. Ongoing work on areas including polymer design, protein labelling and microfluidic technologies will ensure continued progress on improving resolution and throughput, providing deeper understanding of this most important group of targets.

Keywords: Membrane proteins; Native nanodiscs; SMALP; Styrene-maleic acid; Transmembrane protein.

Publication types

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

MeSH terms

  • Lipid Bilayers / chemistry*
  • Membrane Lipids / chemistry*
  • Membrane Proteins / chemistry*
  • Nanostructures / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular*

Substances

  • Lipid Bilayers
  • Membrane Lipids
  • Membrane Proteins