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NMR processing:
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NOEs:
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GeNMR
Cyana
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UNIO ATNOS-Candid
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Fragment-based:
BMRB CS-Rosetta
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Template-based:
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Refinement:
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Structure from chemical shifts:
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WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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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:
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:
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Default Analyzing protein structures in their native environment - R & D Magazine


R & D Magazine


Analyzing protein structures in their native environment
R & D Magazine
However, using a new technique known as sensitivity-enhanced nuclear magnetic resonance (NMR), Massachusetts Institute of Technology (MIT) researchers have shown that they can analyze the structure that a yeast protein forms as it interacts with other ...



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