Solid-state NMR study of the SH3 domain of ?-spectrin: application of13C-15N TEDOR and REDOR (Q62575722)

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Ingolf Sack

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Hans-Heinrich Limbach

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Jutta Pauli

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Mark Kelly

Magnetic Resonance in Chemistry

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publication date

2000

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published in

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volume

38

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issue

7

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page(s)

596-603

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cites work

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Nuclear Magnetic Resonance Spectra from a Crystal rotated at High Speed

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Evidence by15N CPMAS and15N−13C REDOR NMR for Fixation of Atmospheric CO2by Amino Groups of Biopolymers in the Solid State

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Deuterium REDOR: principles and applications for distance measurements

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Structural constraints on the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase from rotational-echo double-resonance NMR.

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Ligand geometry of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase from rotational-echo double-resonance NMR

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Intersubunit communication in tryptophan synthase by carbon-13 and fluorine-19 REDOR NMR.

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Solution structure and peptide binding of the SH3 domain from human Fyn

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1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure

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SH3--an abundant protein domain in search of a function

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