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NMR processing:
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Side-chains:
UNIO ATNOS-Ascan
NOEs:
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ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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UNIO Shiftinspector
LACS
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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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What-If
iCing
PSVS
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SAVES2 or SAVES4
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
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Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
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 More than a third of our proteins are still a mystery for scientists - HealthCanal.co

More than a third of our proteins are still a mystery for scientists - HealthCanal.com



More than a third of our proteins are still a mystery for scientists
HealthCanal.com
Several tools to study the structure of these proteins are already available, such as Nuclear Magnetic Resonance and Small-angle X-ray Scattering (SAXS); ...


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