An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins (Q28239344)

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scientific article (publication date: May 1991)

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English	An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins	scientific article (publication date: May 1991)

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scholarly article

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title

An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins (English)

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author

Mitsuhiko Ikura

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M Ikura

series ordinal

2

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Ad Bax

series ordinal

1

object named as

A Bax

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language of work or name

English

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publication date

May 1991

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published in

Journal of Biomolecular NMR

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volume

1

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issue

1

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page(s)

99-104

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cites work

Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins

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Crossref

reference URL

https://api.crossref.org/works/10.1007%2FBF01874573

retrieved

21 January 2018

The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins

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stated in

Crossref

reference URL

https://api.crossref.org/works/10.1007%2FBF01874573

retrieved

21 January 2018

A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/1668719

retrieved

12 December 2020

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Concerted two-dimensional NMR approaches to hydrogen-1, carbon-13, and nitrogen-15 resonance assignments in proteins

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/1668719

retrieved

12 December 2020

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Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/1668719

retrieved

12 December 2020

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Peptide hydrogen bonding. Conformation dependence of the carbonyl carbon-13 nuclear magnetic resonance chemical shifts in ferrichrome. A study by 13C-[15N] Fourier double resonance spectroscopy1a

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stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/1668719

retrieved

12 December 2020

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Identifiers

DOI

10.1007/BF01874573

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PubMed publication ID

1668719

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