(Q57102724)

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Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations

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Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations (English)

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M Hong

1

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K Jakes

series ordinal

2

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language of work or name

English

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publication date

May 1999

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published in

Journal of Biomolecular NMR

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volume

14

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issue

1

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page(s)

71-4

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cites work

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

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PubMed

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Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width

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High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR.

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12 December 2020

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Improved labeling strategy for 13C relaxation measurements of methyl groups in proteins.

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Determination of membrane protein structure by rotational resonance NMR: bacteriorhodopsin.

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NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein

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Crystal structure of colicin Ia

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Structure-function of the channel-forming colicins

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NMR structural studies of membrane proteins

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https://pubmed.ncbi.nlm.nih.gov/10382307

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Translocation of inserted foreign epitopes by a channel-forming protein

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10382307

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(Q57102724)

Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations

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