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NMR processing:
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NMR assignment:
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PINE
Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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Fragment-based:
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Template-based:
GeNMR
I-TASSER
Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
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MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
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PSVS
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SAVES2 or SAVES4
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NMR spectrum prediction:
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Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
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Unread 03-06-2015, 12:45 AM
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Default 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 Articles 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.

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]



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