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Refinement:
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Structure from chemical shifts:
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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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Chemical shifts re-referencing:
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Molecular dynamics:
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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:
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Isotope labeling:
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Solid-state NMR:
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Default Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.

Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.

Related Articles Nano-mole scale sequential signal assignment by (1)H-detected protein solid-state NMR.

Chem Commun (Camb). 2015 Aug 28;

Authors: Wang S, Parthasarathy S, Xiao Y, Nishiyama Y, Long F, Matsuda I, Endo Y, Nemoto T, Yamauchi K, Asakura T, Takeda M, Terauchi T, Kainosho M, Ishii Y

Abstract
We present a 3D (1)H-detected solid-state NMR (SSNMR) approach for main-chain signal assignments of 10-100 nmol of fully protonated proteins using ultra-fast magic-angle spinning (MAS) at ~80 kHz by a novel spectral-editing method, which permits drastic spectral simplification. The approach offers ~110 fold time saving over a traditional 3D (13)C-detected SSNMR approach.


PMID: 26317132 [PubMed - as supplied by publisher]



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