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NMR processing:
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Side-chains:
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NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
Fragment-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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From structure:
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
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Isotope labeling:
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Default NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.

NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.

Related Articles NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.

Biochemistry. 2001 May 8;40(18):5414-21

Authors: MacRaild CA, Hatters DM, Howlett GJ, Gooley PR

The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints, with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.

PMID: 11331005 [PubMed - indexed for MEDLINE]



Source: PubMed
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