(Q40576237)

21 September 2017

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title

Multidimensional heteronuclear nuclear magnetic resonance of proteins (English)

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21 September 2017

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21 September 2017

Clore GM

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21 September 2017

language of work or name

English

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publication date

1 January 1994

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21 September 2017

published in

Methods in Enzymology

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21 September 2017

volume

239

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21 September 2017

page(s)

349-363

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Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy

21 September 2017

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Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy

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Two-dimensional NMR and protein structure.

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Protein structure determination in solution by two-dimensional and three-dimensional nuclear magnetic resonance spectroscopy

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Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy

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Two-, three-, and four-dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution.

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Comparison of the solution nuclear magnetic resonance and X-ray crystal structures of human recombinant interleukin-1β

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Combining experimental information from crystal and solution studies: joint X-ray and NMR refinement

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Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy.

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High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution

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Three-dimensional NMR spectroscopy of a protein in solution

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Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination

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Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: applicati

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Four-dimensional carbon-13/carbon-13-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1.beta

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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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Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR

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Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy.

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Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy

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Human interleukin 4. The solution structure of a four-helix bundle protein

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The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy

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Solution structure of a calmodulin-target peptide complex by multidimensional NMR

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Solution structure of the cyclosporin A/cyclophilin complex by NMR

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10.1016/S0076-6879(94)39013-4

Identifiers

DOI

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21 September 2017

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