Ile, Leu, and Val Methyl Assignments of the 723-Residue Malate Synthase G Using a New Labeling Strategy and Novel NMR Methods-Reference-Cited by-同舟云学术

Ile, Leu, and Val Methyl Assignments of the 723-Residue Malate Synthase G Using a New Labeling Strategy and Novel NMR Methods

Published:2003-10-16 Issue:45 Volume:125 Page:13868-13878
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Tugarinov Vitali¹,Kay Lewis E.¹

Affiliation:

1. Contribution from the Protein Engineering Network Centres of Excellence and the Departments of Medical Genetics, Biochemistry, and Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja030345s

Reference51 articles.

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2. Farmer, B. T.; Venters, R. A. InNMR of perdeuterated large proteins; Krishna, N. R., Berliner, L. J., Eds.; Kluwer Academic/Plenum Publishers: New York, 1998; Vol. 16, pp 75−120.

3. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

4. NMR Assignment and Secondary Structure Determination of an Octameric 110 kDa Protein Using TROSY in Triple Resonance Experiments

5. Four-Dimensional NMR Spectroscopy of a 723-Residue Protein: Chemical Shift Assignments and Secondary Structure of Malate Synthase G

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