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Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a cavity mutant of T4 lysozyme.
Skrynnikov NR, Mulder FA, Hon B, Dahlquist FW, Kay LE. Skrynnikov NR, et al. J Am Chem Soc. 2001 May 16;123(19):4556-66. doi: 10.1021/ja004179p. J Am Chem Soc. 2001. PMID: 11457242
A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups.
Xu J, Millet O, Kay LE, Skrynnikov NR. Xu J, et al. Among authors: skrynnikov nr. J Am Chem Soc. 2005 Mar 9;127(9):3220-9. doi: 10.1021/ja040215z. J Am Chem Soc. 2005. PMID: 15740163
Estimating the accuracy of protein structures using residual dipolar couplings.
Simon K, Xu J, Kim C, Skrynnikov NR. Simon K, et al. Among authors: skrynnikov nr. J Biomol NMR. 2005 Oct;33(2):83-93. doi: 10.1007/s10858-005-2601-7. J Biomol NMR. 2005. PMID: 16258827
Observation of microsecond time-scale protein dynamics in the presence of Ln3+ ions: application to the N-terminal domain of cardiac troponin C.
Eichmüller C, Skrynnikov NR. Eichmüller C, et al. Among authors: skrynnikov nr. J Biomol NMR. 2007 Feb;37(2):79-95. doi: 10.1007/s10858-006-9105-y. Epub 2006 Dec 19. J Biomol NMR. 2007. PMID: 17180551
Asymmetric doublets in MAS NMR: coherent and incoherent mechanisms.
Skrynnikov NR. Skrynnikov NR. Magn Reson Chem. 2007 Dec;45 Suppl 1:S161-73. doi: 10.1002/mrc.2162. Magn Reson Chem. 2007. PMID: 18157846
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