Send to

Choose Destination
Biochim Biophys Acta. 2016 Oct;1858(10):2549-2557. doi: 10.1016/j.bbamem.2016.02.039. Epub 2016 Mar 3.

Encapsulated membrane proteins: A simplified system for molecular simulation.

Author information

School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
School of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, UK.
Department of Chemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.
School of Life & Health Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
School of Chemical Engineering, College of Engineering and Physical Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK. Electronic address:


Over the past 50years there has been considerable progress in our understanding of biomolecular interactions at an atomic level. This in turn has allowed molecular simulation methods employing full atomistic modelling at ever larger scales to develop. However, some challenging areas still remain where there is either a lack of atomic resolution structures or where the simulation system is inherently complex. An area where both challenges are present is that of membranes containing membrane proteins. In this review we analyse a new practical approach to membrane protein study that offers a potential new route to high resolution structures and the possibility to simplify simulations. These new approaches collectively recognise that preservation of the interaction between the membrane protein and the lipid bilayer is often essential to maintain structure and function. The new methods preserve these interactions by producing nano-scale disc shaped particles that include bilayer and the chosen protein. Currently two approaches lead in this area: the MSP system that relies on peptides to stabilise the discs, and SMALPs where an amphipathic styrene maleic acid copolymer is used. Both methods greatly enable protein production and hence have the potential to accelerate atomic resolution structure determination as well as providing a simplified format for simulations of membrane protein dynamics. This article is part of a Special Issue entitled: Biosimulations edited by Ilpo Vattulainen and Tomasz Róg.


Amphipols; Detergent-free; Lipid bilayer; Membrane proteins (MP); Membrane scaffold proteins (MSP); Nanodiscs; Styrene maleic acid lipid particles (SMALPs)

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center