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Elliptical structure of phospholipid bilayer nanodiscs encapsulated by scaffold proteins: casting the roles of the lipids and the protein.

Phospholipid bilayers host and support the function of membrane proteins and may be stabilized in disc-like nanostructures, allowing for unprecedented solution studies of the assembly, structure, and function of membrane proteins (Bayburt et al. Nano Lett. 2002, 2, 853-856). Based on small-angle neu... Full description

Journal Title: Journal of the American Chemical Society October 6, 2010, Vol.132(39), pp.13713-13722
Main Author: Skar-Gislinge, Nicholas
Other Authors: Simonsen, Jens Bæk , Mortensen, Kell , Feidenhans'L, Robert , Sligar, Stephen G , Lindberg Møller, Birger , Bjørnholm, Thomas , Arleth, Lise
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/ja1030613
Link: http://search.proquest.com/docview/756297835/?pq-origsite=primo
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title: Elliptical structure of phospholipid bilayer nanodiscs encapsulated by scaffold proteins: casting the roles of the lipids and the protein.
format: Article
creator:
  • Skar-Gislinge, Nicholas
  • Simonsen, Jens Bæk
  • Mortensen, Kell
  • Feidenhans'L, Robert
  • Sligar, Stephen G
  • Lindberg Møller, Birger
  • Bjørnholm, Thomas
  • Arleth, Lise
subjects:
  • Lipid Bilayers–Chemistry
  • Membrane Proteins–Chemistry
  • Models, Molecular–Chemistry
  • Models, Theoretical–Chemistry
  • Nanostructures–Chemistry
  • Phospholipids–Chemistry
  • Protein Conformation–Chemistry
  • Lipid Bilayers
  • Membrane Proteins
  • Phospholipids
ispartof: Journal of the American Chemical Society, October 6, 2010, Vol.132(39), pp.13713-13722
description: Phospholipid bilayers host and support the function of membrane proteins and may be stabilized in disc-like nanostructures, allowing for unprecedented solution studies of the assembly, structure, and function of membrane proteins (Bayburt et al. Nano Lett. 2002, 2, 853-856). Based on small-angle neutron scattering in combination with variable-temperature studies of synchrotron small-angle X-ray scattering on nanodiscs in solution, we show that the fundamental nanodisc unit, consisting of a lipid bilayer surrounded by amphiphilic scaffold proteins, possesses intrinsically an elliptical shape. The temperature dependence of the curvature of the nanodiscs prepared with two different phospholipid types (DLPC and POPC) shows that it is the scaffold protein that determines the overall elliptical shape and that the nanodiscs become more circular with increasing temperature. Our data also show that the hydrophobic bilayer thickness is, to a large extent, dictated by the scaffolding protein and adjusted to minimize the hydrophobic mismatch between protein and phospholipid. Our conclusions result from a new comprehensive and molecular-based model of the nanodisc structure and the use of this to analyze the experimental scattering profile from nanodiscs. The model paves the way for future detailed structural studies of functional membrane proteins encapsulated in nanodiscs.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; DOI: 1520-5126 ; DOI: 10.1021/ja1030613
fulltext: no_fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


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titleElliptical structure of phospholipid bilayer nanodiscs encapsulated by scaffold proteins: casting the roles of the lipids and the protein.
creatorSkar-Gislinge, Nicholas ; Simonsen, Jens Bæk ; Mortensen, Kell ; Feidenhans'L, Robert ; Sligar, Stephen G ; Lindberg Møller, Birger ; Bjørnholm, Thomas ; Arleth, Lise
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subjectLipid Bilayers–Chemistry ; Membrane Proteins–Chemistry ; Models, Molecular–Chemistry ; Models, Theoretical–Chemistry ; Nanostructures–Chemistry ; Phospholipids–Chemistry ; Protein Conformation–Chemistry ; Lipid Bilayers ; Membrane Proteins ; Phospholipids
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descriptionPhospholipid bilayers host and support the function of membrane proteins and may be stabilized in disc-like nanostructures, allowing for unprecedented solution studies of the assembly, structure, and function of membrane proteins (Bayburt et al. Nano Lett. 2002, 2, 853-856). Based on small-angle neutron scattering in combination with variable-temperature studies of synchrotron small-angle X-ray scattering on nanodiscs in solution, we show that the fundamental nanodisc unit, consisting of a lipid bilayer surrounded by amphiphilic scaffold proteins, possesses intrinsically an elliptical shape. The temperature dependence of the curvature of the nanodiscs prepared with two different phospholipid types (DLPC and POPC) shows that it is the scaffold protein that determines the overall elliptical shape and that the nanodiscs become more circular with increasing temperature. Our data also show that the hydrophobic bilayer thickness is, to a large extent, dictated by the scaffolding protein and adjusted to minimize the hydrophobic mismatch between protein and phospholipid. Our conclusions result from a new comprehensive and molecular-based model of the nanodisc structure and the use of this to analyze the experimental scattering profile from nanodiscs. The model paves the way for future detailed structural studies of functional membrane proteins encapsulated in nanodiscs.
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