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NMR processing:
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PINE
Side-chains:
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NOEs:
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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:
Preditor
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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:
Shiftcor
UNIO Shiftinspector
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NMR model quality:
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iCing
RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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What-If
iCing
PSVS
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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PPM
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From sequence:
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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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Default NMR analysis of low-density lipoprotein oxidatively-modified in vitro.

NMR analysis of low-density lipoprotein oxidatively-modified in vitro.

Related Articles NMR analysis of low-density lipoprotein oxidatively-modified in vitro.

Free Radic Res Commun. 1990;8(3):175-83

Authors: Barenghi L, Bradamante S, Giudici GA, Vergani C

Human plasma low density lipoprotein has been oxidized at different stages in vitro and analysed by 1H, 13C, and 31P NMR spectroscopy and by biochemical methods. Information was obtained on: a) structure mobilities of lipids and on lipid-protein interactions; b) conjugated and oxo-dienes; c) polyunsaturated/monounsaturated fatty acid chains; d) lysophosphatidylcholine production. The results show that the NMR approach is particularly useful for the assessment of structural modification in oxidized LDL.

PMID: 2328928 [PubMed - indexed for MEDLINE]



Source: PubMed
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