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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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Refinement:
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Structure from chemical shifts:
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WeNMR CS-Rosetta
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Interactions 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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RDCs:
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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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ShiftS
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PPM
CheShift-2- Cα
From sequence:
Shifty
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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
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Isotope labeling:
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Solid-state NMR:
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Old 10-09-2015, 04:49 PM
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Default Enhanced-sensitivity NMR could reveal new clues to how proteins fold - Phys.Org

Enhanced-sensitivity NMR could reveal new clues to how proteins fold - Phys.Org


Phys.Org


Enhanced-sensitivity NMR could reveal new clues to how proteins fold
Phys.Org
Until now, it has been difficult to fully characterize the different structures that proteins can take on in their natural environments. However, using a new technique known as sensitivity-enhanced nuclear magnetic resonance (NMR), MIT researchers have ...

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