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Ab initio:
GeNMR
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Refinement:
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Structure from chemical shifts:
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Flexibility from chemical shifts:
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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:
camLILA
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Isotope labeling:
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Solid-state NMR:
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Default Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectro

Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.

Related Articles Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.

J Am Chem Soc. 2004 Sep 22;126(37):11422-3

Authors: Giraud N, Böckmann A, Lesage A, Penin F, Blackledge M, Emsley L

Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state.

PMID: 15366872 [PubMed - indexed for MEDLINE]



Source: PubMed
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