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NMR processing:
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Side-chains:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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NMR model quality:
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RDCs:
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V-NMR
Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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ArShift- Aromatic
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PPM
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Old 08-22-2010, 05:08 PM
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Default Assessment of cholesteryl ester transfer protein function in lipoprotein mixtures by

Assessment of cholesteryl ester transfer protein function in lipoprotein mixtures by 1H NMR spectroscopy.

Related Articles Assessment of cholesteryl ester transfer protein function in lipoprotein mixtures by 1H NMR spectroscopy.

NMR Biomed. 1997 Oct;10(7):303-8

Authors: Korhonen A, Ala-Korpela M, Liinamaa MJ, Jokisaari J, Kesäniemi YA, Savolainen MJ

Studies of cholesteryl ester transfer protein (CETP) function in lipoprotein mixtures pose many difficulties by conventional biochemical methods. For instance, studies on the effects of CETP on the composition of apolipoprotein B containing lipoproteins (very low and low density lipoproteins) in lipoprotein mixtures are tedious due to repeated ultracentrifugational isolations and have thus rarely been performed. Here we present a new 1H NMR spectroscopy technique to assess the CETP function in lipoprotein mixtures. This technique does not require repeated physical isolations of the lipoprotein particles but uses mathematical separation of the fractions on the basis of biochemical prior knowledge based lineshape fitting analysis of specific lipid resonances in the 1H NMR spectra. The lipoproteins are separated according to their size related chemical shift which allows for distinct quantification between very low and low density lipoproteins, the two major apolipoprotein B containing fractions. The methodological basis of the technique is discussed here together with a demonstration that this kind of approach allows dynamic follow up of the lipid transfer reactions in complex lipoprotein and CETP mixtures. The results revealed a consistent behaviour which corroborated the recent findings suggesting that the neutral lipid mass transfer among lipoproteins is not an equimolar heteroexchange.

PMID: 9471120 [PubMed - indexed for MEDLINE]



Source: PubMed
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