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NMR processing:
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Side-chains:
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GeNMR
Cyana
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Structure from chemical shifts:
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WeNMR CS-Rosetta
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CS23D
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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
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iCing
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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
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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:
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Protein solubility:
camLILA
ccSOL
Camfold
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Isotope labeling:
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Default Journal Highlight: Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

Journal Highlight: Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases

Current research on the role of copper in the conformational changes associated with prion diseases are reviewed with emphasis on the latest applications of NMR and EPR spectroscopy to probe the interactions of copper with prion proteins.

Read the rest at Spectroscopynow.com
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