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NMR processing:
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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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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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RDCs:
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Pseudocontact shifts:
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Protein geomtery:
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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:
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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 04-23-2014, 06:31 PM
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Default Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.

Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.

Related Articles Frontispiece: probing transient conformational States of proteins by solid-state r1? relaxation-dispersion NMR spectroscopy.

Angew Chem Int Ed Engl. 2014 Apr 22;53(17)

Authors: Ma P, Haller JD, Zajakala J, Macek P, Sivertsen AC, Willbold D, Boisbouvier J, Schanda P

Abstract
In their Communication on page 4312 ff., P. Schanda et al. describe an NMR method used to probe conformational states of proteins. Information about the exchange kinetics, relative populations, and structures of the short-lived state can be obtained.


PMID: 24753203 [PubMed - in process]



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