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Side-chains:
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Ab initio:
GeNMR
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Template-based:
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Refinement:
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Structure from chemical shifts:
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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
ccSOL
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Isotope labeling:
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Solid-state NMR:
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Old 12-08-2015, 08:28 PM
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Default Restoring Resolution in Biological Solid-State NMR under Conditions of Off-Magic-Angle Spinning.

Restoring Resolution in Biological Solid-State NMR under Conditions of Off-Magic-Angle Spinning.

Related Articles Restoring Resolution in Biological Solid-State NMR under Conditions of Off-Magic-Angle Spinning.

J Phys Chem Lett. 2015 Dec 7;:5040-5044

Authors: Sarkar R, Rodriguez Camargo DC, Pintacuda G, Reif B

Abstract
Spin-state-selective excitation (S3E) experiments allow the selection of individual transitions in a coupled two spin system. We show that in the solid state, the dipole-dipole interaction (DD) between (15)N and (1)H in a (1)H-(15)N bond and the chemical shift anisotropy (CSA) of (15)N in an amide moiety mutually cancel each other for a particular multiplet component at high field, when the sample is spun off the magic angle (Arctan [?2] = 54.74°). The accuracy of the adjustment of the spinning angle is crucial in conventional experiments. We demonstrate that for S3E experiments, the requirement to spin the sample exactly at the magic angle is not mandatory. Applications of solid state NMR in narrow bore magnets will be facilitated where the adjustment of the magic angle is often difficult. The method opens new perspectives for the development of schemes to determine distances and to quantify dynamics in the solid state.


PMID: 26641130 [PubMed - as supplied by publisher]



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