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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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Ab initio:
GeNMR
Cyana
XPLOR-NIH
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UNIO ATNOS-Candid
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
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PECAN
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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iCing
RDCs:
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Protein geomtery:
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iCing
PSVS
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SAVES2 or SAVES4
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NMR spectrum prediction:
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Flexibility from structure:
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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 Cryo-electron microscopy: Alzheimer's fibrils

Cryo-electron microscopy: Alzheimer's fibrils

A technique that can augment X-ray crystallographic and spectroscopic studies has been demonstrated to provide an atomic resolution in imaging of the amyloid fibrils present in Alzheimer's disease, thanks to European research.

Read the rest at Spectroscopynow.com
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