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Ab initio:
GeNMR
Cyana
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
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Homology-based:
CS23D
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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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Chemical shifts re-referencing:
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Methyl S2
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Molecular dynamics:
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From structure:
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PPM
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
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camGroEL
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Isotope labeling:
UPLABEL
Solid-state NMR:
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Default Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.

Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.

Related Articles Formation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.

Chembiochem. 2013 Sep 23;14(14):1891-7

Authors: Bertini I, Gallo G, Korsak M, Luchinat C, Mao J, Ravera E

Abstract
The accumulation of soluble toxic beta-amyloid (A?) aggregates is an attractive hypothesis for the role of this peptide in the pathology of Alzheimer's disease. We have introduced sedimentation through ultracentrifugation, either by magic angle spinning (in situ) or preparative ultracentrifuge (ex situ), to immobilize biomolecules and make them amenable for solid-state NMR studies (SedNMR). In situ SedNMR is used here to address the kinetics of formation of soluble A? assemblies by monitoring the disappearance of the monomer and the appearance of the oligomers simultaneously. Ex situ SedNMR allows us to select different oligomeric species and to reveal atomic-level structural features of soluble A? assemblies.


PMID: 23821412 [PubMed - indexed for MEDLINE]



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