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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Cross-Correlated Relaxation Enhanced 1H−13C NMR Spectroscopy of Methyl Groups in Very High Molecular Weight Proteins and Protein Complexes

Tugarinov, Vitali, Hwang, Peter M., Ollerenshaw, Jason E., Kay, Lewis E.·2003·Journal of the American Chemical Society

Abstract

A comparison of HSQC and HMQC pulse schemes for recording (1)H[bond](13)C correlation maps of protonated methyl groups in highly deuterated proteins is presented. It is shown that HMQC correlation maps can be as much as a factor of 3 more sensitive than their HSQC counterparts and that the sensitivity gains result from a TROSY effect that involves cancellation of intra-methyl dipolar relaxation interactions. (1)H[bond](13)C correlation spectra are recorded on U-[(15)N,(2)H], Ile delta 1-[(13)C,(1)H] samples of (i) malate synthase G, a 723 residue protein, at 37 and 5 degrees C, and of (ii) the protease ClpP, comprising 14 identical subunits, each with 193 residues (305 kDa), at 5 degrees C. The high quality of HMQC spectra obtained in short measuring times strongly suggests that methyl groups will be useful probes of structure and dynamics in supramolecular complexes.

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Metadata

Authors
Tugarinov, V., Hwang, P. M., Ollerenshaw, J. E., & Kay, L. E.
Venue
Journal of the American Chemical Society
Published
2003-08-01
Volume
125
Issue
34
Pages
10420-10428
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
OpenAlex
W2074856155
Cited by
649
References
1
FWCI
4.85
Type
journal article
Language
en
Open access
closed

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