title: Encapsulated membrane proteins: A simplified system for molecular simulation.
abstract: 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.
authors.affiliation: School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
authors.forename: Sarah C
authors.initials: SC
authors.lastname: Lee
authors.affiliation: School of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, UK.
authors.forename: Syma
authors.initials: S
authors.lastname: Khalid
authors.affiliation: School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
authors.forename: Naomi L
authors.initials: NL
authors.lastname: Pollock
authors.affiliation: School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
authors.forename: Tim J
authors.initials: TJ
authors.lastname: Knowles
authors.affiliation: Department of Chemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.
authors.forename: Karen
authors.initials: K
authors.lastname: Edler
authors.affiliation: School of Life & Health Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK.
authors.forename: Alice J
authors.initials: AJ
authors.lastname: Rothnie
authors.affiliation: School of Chemical Engineering, College of Engineering and Physical Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
authors.forename: Owen
authors.initials: O
authors.lastname: R T Thomas
authors.affiliation: School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK. Electronic address: T.R.Dafforn@Bham.ac.uk.
authors.forename: Timothy R
authors.initials: TR
authors.lastname: Dafforn
mesh_terms: D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D053758:Nanoparticles; D044367:Phase Transition
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins
keywords: Amphipols; Detergent-free; Lipid bilayer; Membrane proteins (MP); Membrane scaffold proteins (MSP); Nanodiscs; Styrene maleic acid lipid particles (SMALPs)