Thread: NMR paper Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
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Default Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Quenched Hydrogen Exchange NMR of Amyloid Fibrils.

Related Articles Quenched Hydrogen Exchange NMR of Amyloid Fibrils.

Methods Mol Biol. 2016;1345:211-22

Authors: Alexandrescu AT

Abstract
Amyloid fibrils are associated with a number of human diseases. These aggregatively misfolded intermolecular ?-sheet assemblies constitute some of the most challenging targets in structural biology because to their complexity, size, and insolubility. Here, protocols and controls are described for experiments designed to study hydrogen-bonding in amyloid fibrils indirectly, by transferring information about amide proton occupancy in the fibrils to the dimethyl sulfoxide-denatured state. Since the denatured state is amenable to solution NMR spectroscopy, the method can provide residue-level-resolution data on hydrogen exchange for the monomers that make up the fibrils.


PMID: 26453215 [PubMed - in process]



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