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NMR processing:
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Side-chains:
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NOEs:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
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Fragment-based:
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Structure from chemical shifts:
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WeNMR CS-Rosetta
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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
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NMR model quality:
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RDCs:
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Protein geomtery:
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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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CheShift-2- Cα
From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
Validate NMR-STAR 3.1
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 03-31-2014, 10:16 AM
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Default Journal Highlight: NMR structures of fusion peptide from influenza hemagglutinin H3 subtype and its mutants

Journal Highlight: NMR structures of fusion peptide from influenza hemagglutinin H3 subtype and its mutants

The structures of the influenza hemagglutinin H3-HAfp23 peptide and its mutants, G1S and G1V, in dodecylphosphatidyl choline micelles were studied by heteronuclear NMR spectroscopy to study the role of its amino acids in the fusion process.

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