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Ab initio:
GeNMR
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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:
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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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Protein geomtery:
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NMR spectrum prediction:
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From sequence:
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
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Isotope labeling:
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Solid-state NMR:
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Old 11-24-2010, 08:58 PM
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Default Solid-state NMR and rigid body molecular dynamics to determine domain orientations of

Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban.

Related Articles Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban.

J Am Chem Soc. 2002 Aug 14;124(32):9392-3

Authors: Mascioni A, Karim C, Zamoon J, Thomas DD, Veglia G

Solid-state NMR spectroscopy, in conjunction with rigid body molecular dynamics calculations, shows that monomeric phospholamban in lipid bilayers has two distinct helical domains, with an interhelical angle within 60-100 degrees, ruling out the possibility of a continuous alpha-helical structure for this protein.

PMID: 12167032 [PubMed - indexed for MEDLINE]



Source: PubMed
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