Tugarinov V - Search Results

1

Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods.

Tugarinov V, Kay LE. Tugarinov V, et al. J Am Chem Soc. 2003 Nov 12;125(45):13868-78. doi: 10.1021/ja030345s. J Am Chem Soc. 2003. PMID: 14599227

2

Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase g.

Tugarinov V, Muhandiram R, Ayed A, Kay LE. Tugarinov V, et al. J Am Chem Soc. 2002 Aug 28;124(34):10025-35. doi: 10.1021/ja0205636. J Am Chem Soc. 2002. PMID: 12188667

3

Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G.

Tugarinov V, Kay LE. Tugarinov V, et al. J Mol Biol. 2003 Apr 11;327(5):1121-33. doi: 10.1016/s0022-2836(03)00238-9. J Mol Biol. 2003. PMID: 12662935

4

Side chain assignments of Ile delta 1 methyl groups in high molecular weight proteins: an application to a 46 ns tumbling molecule.

Tugarinov V, Kay LE. Tugarinov V, et al. J Am Chem Soc. 2003 May 14;125(19):5701-6. doi: 10.1021/ja021452+. J Am Chem Soc. 2003. PMID: 12733908

5

Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE. Tugarinov V, et al. J Am Chem Soc. 2003 Aug 27;125(34):10420-8. doi: 10.1021/ja030153x. J Am Chem Soc. 2003. PMID: 12926967

6

An isotope labeling strategy for methyl TROSY spectroscopy.

Tugarinov V, Kay LE. Tugarinov V, et al. J Biomol NMR. 2004 Feb;28(2):165-72. doi: 10.1023/B:JNMR.0000013824.93994.1f. J Biomol NMR. 2004. PMID: 14755160

These enhancements derive from a TROSY effect in which complete cancellation of intra-methyl (1)H-(1)H and (1)H-(13)C dipolar interactions occurs for 50% of the signal in the case of HMQC, so long as the methyl is attached to a molecule tumbling in the macromolecular limit (Tu …

These enhancements derive from a TROSY effect in which complete cancellation of intra-methyl (1)H-(1)H and (1)H-(13)C dipolar interactions o …

7

Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme.

Korzhnev DM, Kloiber K, Kanelis V, Tugarinov V, Kay LE. Korzhnev DM, et al. Among authors: tugarinov v. J Am Chem Soc. 2004 Mar 31;126(12):3964-73. doi: 10.1021/ja039587i. J Am Chem Soc. 2004. PMID: 15038751

The experiment benefits from a methyl-TROSY effect in which cancellation of intramethyl dipole fields occurs, leading to methyl (13)C-(1)H correlation spectra of high sensitivity and resolution (Tugarinov, V.; Hwang, P. M.; Ollerenshaw, J. E.; Kay, L. E. J. Am. ...

The experiment benefits from a methyl-TROSY effect in which cancellation of intramethyl dipole fields occurs, leading to methyl (13)C-(1)H c …

8

Line narrowing in methyl-TROSY using zero-quantum 1H-13C NMR spectroscopy.

Tugarinov V, Sprangers R, Kay LE. Tugarinov V, et al. J Am Chem Soc. 2004 Apr 21;126(15):4921-5. doi: 10.1021/ja039732s. J Am Chem Soc. 2004. PMID: 15080697

9

Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins.

Tugarinov V, Hwang PM, Kay LE. Tugarinov V, et al. Annu Rev Biochem. 2004;73:107-46. doi: 10.1146/annurev.biochem.73.011303.074004. Annu Rev Biochem. 2004. PMID: 15189138 Review.

10

1H,13C-1H,1H dipolar cross-correlated spin relaxation in methyl groups.

Tugarinov V, Kay LE. Tugarinov V, et al. J Biomol NMR. 2004 Jul;29(3):369-76. doi: 10.1023/B:JNMR.0000032562.07475.7f. J Biomol NMR. 2004. PMID: 15213435

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