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NMR processing:
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Side-chains:
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NOEs:
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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:
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Torsion angles from chemical shifts:
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Promega- Proline
Secondary structure from chemical shifts:
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MICS caps, β-turns
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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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Pseudocontact shifts:
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Protein geomtery:
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NMR spectrum prediction:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
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:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
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Solid-state NMR:
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Default Human herpes virus 4: No bar to understanding

Human herpes virus 4: No bar to understanding

NMR spectroscopy has been used to investigate how a viral protein in human herpes virus 4 (also known as Epstein-Barr) regulates the activity of a second essential protein and so reveals a possible new target for the development of antiviral drugs against this common infectious agent.

Read the rest at Spectroscopynow.com
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