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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:
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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:
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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
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Isotope labeling:
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Solid-state NMR:
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Old 10-12-2015, 01:04 AM
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Default Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.

Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.

Related Articles Preparation of Amyloid Fibrils for Magic-Angle Spinning Solid-State NMR Spectroscopy.

Methods Mol Biol. 2016;1345:173-83

Authors: Tuttle MD, Courtney JM, Barclay AM, Rienstra CM

Abstract
Solid-state NMR spectroscopy (SSNMR) is an established and invaluable tool for the study of amyloid fibril structure with atomic-level detail. Optimization of the homogeneity and concentration of fibrils enhances the resolution and sensitivity of SSNMR spectra. Here, we present a fibrillization and fibril processing protocol, starting from purified monomeric ?-synuclein, that enables the collection of high-resolution SSNMR spectra suitable for site-specific structural analysis. This protocol does not rely on any special features of ?-synuclein and should be generalizable to any other amyloid protein.


PMID: 26453212 [PubMed - in process]



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