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NMR processing:
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Side-chains:
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NOEs:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
GeNMR
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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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Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
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NMR model quality:
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Pseudocontact shifts:
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NMR spectrum prediction:
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Flexibility from structure:
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Methyl S2
B-factor
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:
Shifty
Camcoil
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:
sedNMR


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Default A New Class: Protein-Protein Interactions As Drug Targets - Bio-IT World



A New Class: Protein-Protein Interactions As Drug Targets
Bio-IT World
Biophysical techniques such as nuclear magnetic resonance (NMR) and surface plasmon resonance (SPR), which are employed for, among other things, detecting the interaction of molecules with one another in PPI complexes, have become more robust.



A New Class: Protein-Protein Interactions As Drug Targets - Bio-IT World
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