Biomolecular NMR

Group publications

T. Yuwen, Y. Xue, N. R. Skrynnikov, Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets: 2. The Model of Encounter Complex Involving the Double Mutant of the c-Crk N-SH3 Domain and Peptide Sos. Biochemistry. 2016, 55, 1784-1800.

N. R. Skrynnikov, Interview with Robert Tycko: On amyloids, Alzheimer disease, and solid-state NMR. Concepts Magn. Reson., Part A. 2015, 44, 182-189.

P. Ma, Y. Xue, N. Coquelle, J. D. Haller, T. Yuwen, I. Ayala, O. Mikhailovskii, D. Willbold, J. P. Colletier, N. R. Skrynnikov, P. Schanda P, Observing the overall rocking motion of a protein in a crystal. Nat. Commun. 2015, 6:8361. Supplemental: movie I movie II movie III

Y. Xue, T. Yuwen, F. Zhu, N. R. Skrynnikov, Role of Electrostatic Interactions in Binding of Peptides and Intrinsically Disordered Proteins to Their Folded Targets. 1. NMR and MD Characterization of the Complex between the c- Crk N -SH3 Domain and the Peptide Sos. Biochemistry 2014, 53, 6473-6495.

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, ¹⁵N^H/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_1ρ 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