[NMR paper] Buffer-Induced Swelling and Vesicle Budding in Binary Lipid Mixtures of Dioleoylphosphatidylcholine:Dioleoylphosphatidylet hanolamine and Dioleoylphosphatidylcholine:Lysophosphatidylcholin e Using Small-Angle X-ray Scattering and (31)P Static NMR.
Buffer-Induced Swelling and Vesicle Budding in Binary Lipid Mixtures of Dioleoylphosphatidylcholine:Dioleoylphosphatidylet hanolamine and Dioleoylphosphatidylcholine:Lysophosphatidylcholin e Using Small-Angle X-ray Scattering and (31)P Static NMR.
Related ArticlesBuffer-Induced Swelling and Vesicle Budding in Binary Lipid Mixtures of Dioleoylphosphatidylcholine:Dioleoylphosphatidylet hanolamine and Dioleoylphosphatidylcholine:Lysophosphatidylcholin e Using Small-Angle X-ray Scattering and (31)P Static NMR.
Langmuir. 2015 Mar 4;
Authors: Barriga HM, Bazin R, Templer RH, Law RV, Ces O
Abstract
A large variety of data exists on lipid phase behavior; however, it is mostly in nonbuffered systems over nonbiological temperature ranges. We present biophysical data on lipid mixtures of dioleoylphosphatidylcholine (DOPC), dioleoylphosphatidylethanolamine (DOPE), and lysophosphatidylcholine (LysoPC) examining their behaviors in excess water and buffer systems over the temperature range 4-34 °C. These mixtures are commonly used to investigate the effects of spontaneous curvature on integral membrane proteins. Using small-angle X-ray scattering (SAXS) and (31)P NMR, we observed lamellar and vesicle phases, with the buffer causing an increase in the layer spacing. Increasing amounts of DOPE in a DOPC bilayer decreased the layer spacing of the mesophase, while the opposite trend was observed for increasing amounts of LysoPC. (31)P static NMR was used to analyze the DOPC:LysoPC samples to investigate the vesicle sizes present, with evidence of vesicle budding observed at LysoPC concentrations above 30 mol %. NMR line shapes were fitted using an adapted program accounting for the distortion of the lipids within the magnetic field. The distortion of the vesicle, because of magnetic susceptibility, varied with LysoPC content, and a discontinuity was found in both the water and buffer samples. Generally, the distortion increased with LysoPC content; however, at a ratio of DOPC:LysoPC 60:40, the sample showed a level of distortion of the vesicle similar to that of pure DOPC. This implies an increased flexibility in the membrane at this point. Commonly, the assumption is that for increasing LysoPC concentration there is a reduction in membrane tension, implying that estimations of membrane tension based on spontaneous curvature assumptions may not be accurate.
PMID: 25738977 [PubMed - as supplied by publisher]
[NMR paper] Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data.
Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data.
Structural Characterization of a Flexible Two-Domain Protein in Solution Using Small Angle X-Ray Scattering and NMR Data.
Structure. 2014 Nov 6;22(12):1862-1874
Authors: Lemak A, Wu B, Yee A, Houliston S, Lee HW, Gutmanas A, Fang X, Garcia M, Semesi A, Wang YX, Prestegard JH, Arrowsmith CH
Abstract
Multidomain proteins in which individual domains are connected by linkers often possess inherent...
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12-03-2014 04:05 PM
The dynamic duo: Combining NMR and small angle scattering in structural biology
The dynamic duo: Combining NMR and small angle scattering in structural biology
Abstract
Structural biology provides essential information for elucidating molecular mechanisms that underlie biological function. Advances in hardware, sample preparation, experimental methods, and computational approaches now enable structural analysis of protein complexes with increasing complexity that more closely represent biologically entities in the cellular environment. Integrated multidisciplinary approaches are required to overcome limitations of individual methods and take advantage of...
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04-17-2014 12:03 PM
Using Small Angle Solution Scattering Data in Xplor-NIH Structure Calculations
Using Small Angle Solution Scattering Data in Xplor-NIH Structure Calculations
Publication date: Available online 3 April 2014
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Charles D. Schwieters , G. Marius Clore</br>
This contribution describes the use of small and wide angle X-ray and small angle neutron scattering for biomolecular structure calculation using the program Xplor-NIH, both with and without NMR data. The current algorithms used for calculating scattering curves are described, and the use of scattering data as a...
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04-04-2014 01:19 PM
[NMR paper] The Dynamic Duo: Combining NMR and Small Angle Scattering in Structural Biology.
The Dynamic Duo: Combining NMR and Small Angle Scattering in Structural Biology.
The Dynamic Duo: Combining NMR and Small Angle Scattering in Structural Biology.
Protein Sci. 2014 Mar 29;
Authors: Hennig J, Sattler M
Abstract
Structural biology provides essential information for elucidating molecular mechanisms that underlie biological function. Advances in hardware, sample preparation, experimental methods and computational approaches now enable structural analysis of protein complexes with increasing complexity that more...
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04-02-2014 11:54 PM
The Dynamic Duo: Combining NMR and Small Angle Scattering in Structural Biology
The Dynamic Duo: Combining NMR and Small Angle Scattering in Structural Biology
Abstract
Structural biology provides essential information for elucidating molecular mechanisms that underlie biological function. Advances in hardware, sample preparation, experimental methods and computational approaches now enable structural analysis of protein complexes with increasing complexity that more closely represent biologically entities in the cellular environment. Integrated multi-disciplinary approaches are required to overcome limitations of individual methods and take advantage of...
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03-29-2014 01:00 PM
Small Angle X-Ray Scattering and the Determination of Protein Shape - Azom.com
Small Angle X-Ray Scattering and the Determination of Protein Shape - Azom.com
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Small Angle X-Ray Scattering and the Determination of Protein Shape
Azom.com
The low resolution 3D structure obtained by ab-initio methods is an important additional data to the high resolution structures obtained by protein crystallography and NMR. This article discusses the application of SAXSess mc system from Anton Paar to ...
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02-20-2013 06:24 PM
NMR and Small Angle Scattering-based structural analysis of protein complexes in solu
NMR and Small Angle Scattering-based structural analysis of protein complexes in solution.
Related Articles NMR and Small Angle Scattering-based structural analysis of protein complexes in solution.
J Struct Biol. 2010 Nov 10;
Authors: Madl T, Gabel F, Sattler M
Structural analysis of multi-domain protein complexes is a key challenge in current biology and a prerequisite for understanding the molecular basis of essential cellular processes. The use of solution techniques is important for characterizing the quaternary arrangements and dynamics of...
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11-16-2010 04:13 PM
Multidomain Protein Structures from NMR & Solution Small-Angle X-ray Scattering
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Refinement of Multidomain Protein Structures by Combination of Solution Small-Angle X-ray Scattering and NMR Data
Alexander Grishaev,* Justin Wu, Jill Trewhella, and Ad Bax*
Contribution from the Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, Maryland 20892-0520, Department of Biochemistry, The Ohio State University, Columbus, Ohio 43210, and Department of Chemistry, University of Utah, Salt Lake City, Utah 84112-0850
J. Am. Chem. Soc.; 2005; 127(47) pp 16621 -...