Encapsulated membrane proteins : A simplified system for molecular simulation
Lee, Sarah C. ; Khalid, Syma ; Pollock, Naomi L. ; Knowles, Tim J. ; Edler, Karen LU
; Rothnie, Alice J.
; R.T.Thomas, Owen
and Dafforn, Timothy R.
(2016)
In Biochimica et Biophysica Acta - Biomembranes
1858(10).
p.2549-2557
- Abstract
Over the past 50 years 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... (More)
Over the past 50 years 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.
(Less)
- author
- Lee, Sarah C.
; Khalid, Syma
; Pollock, Naomi L.
; Knowles, Tim J.
; Edler, Karen
LU
; Rothnie, Alice J.
; R.T.Thomas, Owen
and Dafforn, Timothy R.
- publishing date
- 2016-10-01
- type
- Contribution to journal
- publication status
- published
- keywords
- Amphipols, Detergent-free, Lipid bilayer, Membrane proteins (MP), Membrane scaffold proteins (MSP), Nanodiscs, Styrene maleic acid lipid particles (SMALPs)
- in
- Biochimica et Biophysica Acta - Biomembranes
- volume
- 1858
- issue
- 10
- pages
- 9 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:26946242
- scopus:84961219078
- ISSN
- 0005-2736
- DOI
- 10.1016/j.bbamem.2016.02.039
- language
- English
- LU publication?
- no
- additional info
- Publisher Copyright: © 2016 Elsevier B.V.
- id
- d184e971-bc03-47b9-b97c-a1285ec2c318
- date added to LUP
- 2023-03-29 11:44:44
- date last changed
- 2024-04-18 19:34:37
@article{d184e971-bc03-47b9-b97c-a1285ec2c318,
abstract = {{<p>Over the past 50 years 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.</p>}},
author = {{Lee, Sarah C. and Khalid, Syma and Pollock, Naomi L. and Knowles, Tim J. and Edler, Karen and Rothnie, Alice J. and R.T.Thomas, Owen and Dafforn, Timothy R.}},
issn = {{0005-2736}},
keywords = {{Amphipols; Detergent-free; Lipid bilayer; Membrane proteins (MP); Membrane scaffold proteins (MSP); Nanodiscs; Styrene maleic acid lipid particles (SMALPs)}},
language = {{eng}},
month = {{10}},
number = {{10}},
pages = {{2549--2557}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta - Biomembranes}},
title = {{Encapsulated membrane proteins : A simplified system for molecular simulation}},
url = {{http://dx.doi.org/10.1016/j.bbamem.2016.02.039}},
doi = {{10.1016/j.bbamem.2016.02.039}},
volume = {{1858}},
year = {{2016}},
}