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NMR processing:
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Side-chains:
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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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Homology-based:
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Torsion angles from chemical shifts:
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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
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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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SAVES2 or SAVES4
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NMR spectrum prediction:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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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:
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Solid-state NMR:
sedNMR


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Default High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.

High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.

Related Articles High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.

J Am Chem Soc. 2005 Jul 27;127(29):10138-9

Authors: Sillen A, Wieruszeski JM, Leroy A, Younes AB, Landrieu I, Lippens G

HRMAS NMR of tau paired helical fragments assembled with heparin show an intensity decrease for those amino acids that are incorporated into the rigid core region, whereas the N-terminal amino acids maintain their full mobility.

PMID: 16028903 [PubMed - indexed for MEDLINE]



Source: PubMed
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