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NMR processing:
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PINE
Side-chains:
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NOEs:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
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UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Promega- Proline
Secondary structure from chemical shifts:
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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:
Shiftcor
UNIO Shiftinspector
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NMR model quality:
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Chemical shifts:
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iCing
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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MetaMQAPII
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STAN
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ERRAT
Verify_3D
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
Backbone S2
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 Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.

Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.

Related Articles Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.

Angew Chem Int Ed Engl. 2012 Oct 8;51(41):10289-92

Authors: Antzutkin ON, Iuga D, Filippov AV, Kelly RT, Becker-Baldus J, Brown SP, Dupree R

PMID: 22976560 [PubMed - indexed for MEDLINE]



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