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NMR processing:
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NMR assignment:
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PINE
Side-chains:
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NOEs:
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
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Fragment-based:
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Template-based:
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Refinement:
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Structure 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
UNIO Shiftinspector
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NMR model quality:
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Protein geomtery:
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What-If
iCing
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SAVES2 or SAVES4
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NMR spectrum prediction:
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Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
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CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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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 Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of ?-synuclein in intact viable cells

Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of ?-synuclein in intact viable cells

The protein ?-syn adopts a wide variety of conformations including an intrinsically disordered monomeric form and an ?-helical rich membrane-associated form that is thought to play an important role in cellular membrane processes. However, despite the high affinity of ?-syn for membranes, evidence that the ?-helical form of ?-syn is adopted inside cells has thus far been indirect. In cell DNP-assisted solid state NMR on frozen samples has the potential to report directly on the entire...

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