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NMR processing:
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Side-chains:
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Structure from NMR restraints:
Ab initio:
GeNMR
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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:
Fragment-based:
WeNMR CS-Rosetta
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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iCing
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NMR spectrum prediction:
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Flexibility from structure:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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From sequence:
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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 Evolution of ?-synuclein conformation ensemble toward amyloid fibril via liquid-liquid phase separation (LLPS) as investigated by dynamic nuclear polarization-enhanced solid-state MAS NMR

Evolution of ?-synuclein conformation ensemble toward amyloid fibril via liquid-liquid phase separation (LLPS) as investigated by dynamic nuclear polarization-enhanced solid-state MAS NMR

Protein fibrillation and human neurodegenerative diseases, with a profound underlying connection suggested between them, have been the subject of intense investigations in the medical, biophysical and bio-engineering sciences. For gaining the molecular mechanistic insights into such connection, i.e., the cause and effect, atomic-resolution molecular structure information especially on the initial oligomeric states is of paramount importance, not only that on the mature amyloid fibrils....

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