Biomolecular NMR

Purdue University

Group publications

T. Yuwen, N. R. Skrynnikov, CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions. J. Biomol. NMR 2014, 58, 175-192.

Y. Xue, N. R. Skrynnikov, Ensemble MD simulations restrained via crystallographic data: accurate structure leads to accurate dynamics. Prot. Sci. 2014, 23, 488-507.

T. Yuwen, N. R. Skrynnikov, Proton-decoupled CPMG: A better experiment for measuring 15N R2 relaxation in disordered proteins. J. Magn. Reson. 2014, 241, 155-169.

J. M. Ward, N. R. Skrynnikov, Very large residual dipolar couplings from deuterated ubiquitin. J. Biomol. NMR 2012, 54, 53-67.

Y. Xue, J. M. Ward, T. Yuwen, I. S. Podkorytov, N. R. Skrynnikov, Microsecond time-scale conformational exchange in proteins: using long Molecular Dynamics trajectory to simulate NMR relaxation dispersion data. J. Am. Chem. Soc. 2012, 134, 2555-2562.

Y. Xue, N. R. Skrynnikov, Motion of a disordered polypeptide chain as studied by paramagnetic relaxation enhancements, 15N relaxation, and Molecular Dynamics simulations: How fast is segmental diffusion in denatured ubiquitin? J. Am. Chem. Soc. 2011, 133, 14614-14628. Supplemental: movie I movie II movie III

T. Yuwen, C. B. Post, N. R. Skrynnikov, Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media? J. Biomol. NMR 2011, 51, 131-150.

V. Chevelkov, Y. Xue, R. Linser, N. R. Skrynnikov, B. Reif, Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics. J. Am. Chem. Soc. 2010, 132, 5015-5017.

V. Chevelkov, Y. Xue, D. Krishna Rao, J. D. Forman-Kay, N. R. Skrynnikov, 15NH/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3. J. Biomol. NMR 2010, 46, 227-244.

J. Xu, Y. Xue, N. R. Skrynnikov, Detection of nanosecond time scale side-chain jumps in a protein dissoloved in water/glycerol solvent. J. Biomol. NMR 2009, 45, 57-72.

Y. Xue, I. S. Podkorytov, D. Krishna Rao, N. Benjamin, H. Sun, N. R. Skrynnikov, Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain. Prot. Sci. 2009, 18, 1401-1424. Supplemental: movie I movie II

V. Agarwal, Y. Xue, B. Reif, N. R. Skrynnikov, Protein side-chain dynamics as observed by solution- and solid-state NMR spectroscopy: a similarity revealed. J. Am. Chem. Soc. 2008, 130, 16611-16621.

N. R. Skrynnikov, Asymmetric doublets in MAS NMR: coherent and incoherent mechanisms. Magn. Reson. Chem., 2007, 45, S161-S173.

V. Chevelkov; A. Zhuravleva; Y. Xue; B. Reif; N. R. Skrynnikov, Combined analysis of 15N relaxation data from solid- and solution-state NMR. J. Am. Chem. Soc., 2007, 129, 12594-12595

Y. E. Ryabov; C. White; Y. Xue; N. R. Skrynnikov, Introducing color into stacking gels makes sample loading easy. Anal. Biochemistry 2007, 366, 111-112.

Y. Xue; M. S. Pavlova; Y. E. Ryabov; B. Reif; N. R. Skrynnikov, Methyl rotation barriers in proteins from 2H relaxation data. Implications for protein structure. J. Am. Chem. Soc. 2007, 129, 6827-6838.

I. S. Podkorytov; N. R. Skrynnikov, Transient NOE-exchange-relay experiment. Application to ligand-protein binding under slow exchange conditions. J. Magn. Reson. 2007, 187, 44-51.

C. Eichmüller; N. R. Skrynnikov, Observation of ms time-scale protein dynamics in the presence of Ln3+ ions: application to the N-terminal domain of cardiac troponin C. J. Biomol. NMR 2007, 37, 79-95.

V. Agarwal; A. Diehl; N. R. Skrynnikov; B. Reif, High resolution proton detected proton-carbon correlation spectra of a protein in MAS solid state NMR spectroscopy.  J. Am. Chem. Soc. 2006, 128, 12620-12621.

V. Kanelis; M. C. Bruce; N. R. Skrynnikov; D. Rotin; J. D. Forman-Kay, Structural Determinants for High Affinity Binding in a Nedd4 WW3* Domain - Comm PY Motif Complex. Structure. 2006, 14, 543-553.

R. Reif; Y. Xue; V. Agarwal; M. S. Pavlova; M. Hologne; A. Diehl; Y. E. Ryabov; N. R. Skrynnikov, Protein side-chain dynamics observed by solution- and solid-state NMR: comparative analysis of methyl 2H relaxation data. J. Am. Chem. Soc. 2006, 128,12354-12355

K. Simon; J. Xu; C. Kim; N. R. Skrynnikov, Estimating the accuracy of protein structures using residual dipolar couplings. J. Biomol. NMR 2005, 33, 83-93

J. E. Ollerenshaw; V. Tugarinov; N. R. Skrynnikov; L. E. Kay, Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins. J. Biomol. NMR. 2005, 33, 25-41.

C. Eichmüller; N. R. Skrynnikov, A new amide proton R experiment permits accurate characterization of microsecond time-scale conformational exchange. J. Biomol. NMR 2005, 32, 281-293

J. Xu; O. Millet; L. E. Kay; N. R. Skrynnikov, A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups. J. Am. Chem. Soc. 2005, 127, 3220-3229

I. S. Podkorytov; N. R. Skrynnikov, Microsecond time-scale dynamics from relaxation in the rotating frame: experiments using spin lock with alternating phase. J. Magn. Reson. 2004, 169, 164-173

N. R. Skrynnikov, Orienting molecular fragments and molecules with residual dipolar couplings. C. R. Physique 2004, 5, 359-375

Find us at WTHR 333A & 352 in WTHR building (map), phone: (765) 496-3324