N. Skrynnikov

发表

Molecular Dynamics model of peptide-protein conjugation: case study of covalent complex between Sos1 peptide and N-terminal SH3 domain from Grb2

D. Luzik, O. Rogacheva, S. A. Izmailov, 2019, Scientific Reports.

Simple MD-based model for oxidative folding of peptides and proteins

S. A. Izmailov, N. Skrynnikov, I. S. Podkorytov, 2017, Scientific Reports.

Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy.

L. Kay, J. Forman-Kay, W. Choy, 2001, Journal of the American Chemical Society.

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.

Fangqiang Zhu, N. Skrynnikov, Yi Xue, 2014, Biochemistry.

Slow conformational exchange and overall rocking motion in ubiquitin protein crystals

I. Ayala, P. Schanda, N. Coquelle, 2017, bioRxiv.

Slow conformational exchange and overall rocking motion in ubiquitin protein crystals

I. Ayala, P. Schanda, N. Coquelle, 2017, Nature Communications.

An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.

L. Kay, D. Torchia, D. Korzhnev, 2002, Journal of the American Chemical Society.

Methyl rotation barriers in proteins from 2H relaxation data. Implications for protein structure.

B. Reif, N. Skrynnikov, Yi Xue, 2007, Journal of the American Chemical Society.

Microsecond time-scale conformational exchange in proteins: using long molecular dynamics trajectory to simulate NMR relaxation dispersion data.

N. Skrynnikov, I. S. Podkorytov, Yi Xue, 2012, Journal of the American Chemical Society.

Slow dynamics in folded and unfolded states of an SH3 domain.

L. Kay, F. Mulder, M. Tollinger, 2001, Journal of the American Chemical Society.

Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy.

L. Kay, V. Tugarinov, R. Muhandiram, 2001, Journal of molecular biology.

Measurement of slow (micros-ms) time scale dynamics in protein side chains by (15)N relaxation dispersion NMR spectroscopy: application to Asn and Gln residues in a cavity mutant of T4 lysozyme.

L. Kay, F. Dahlquist, F. Mulder, 2001, Journal of the American Chemical Society.

Detecting protein kinase recognition modes of calmodulin by residual dipolar couplings in solution NMR.

L. Kay, M. Ikura, K. Yap, 2002, Biochemistry.

Estimating the Accuracy of Protein Structures using Residual Dipolar Couplings

N. Skrynnikov, Jun Xu, Katya Simon, 2005, Journal of biomolecular NMR.

Comparison of 13CH3, 13CH2D, and 13CHD2 methyl labeling strategies in proteins

L. Kay, V. Tugarinov, Jason E. Ollerenshaw, 2005, Journal of biomolecular NMR.

Paramagnetic relaxation enhancements in unfolded proteins: Theory and application to drkN SH3 domain

Honglei Sun, Yi Xue, Honglei Sun, 2009, Protein science : a publication of the Protein Society.

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?

N. Skrynnikov, Yi Xue, 2011, Journal of the American Chemical Society.

What Drives 15N Spin Relaxation in Disordered Proteins? Combined NMR/MD Study of the H4 Histone Tail.

S. A. Izmailov, N. Skrynnikov, I. S. Podkorytov, 2018, Biophysical journal.

Aromatic ring flips in differently packed protein crystals: MAS NMR and MD studies of 3 ubiquitin lattices

Diego F. Gauto, I. Ayala, P. Schanda, 2022 .

Histone Tail

S. A. Izmailov, N. Skrynnikov, I. S. Podkorytov, 2022 .

A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups.

L. Kay, O. Millet, N. Skrynnikov, 2005, Journal of the American Chemical Society.

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.

L. Kay, F. Dahlquist, F. Mulder, 2001, Journal of the American Chemical Society.

EFFECTS OF DYNAMICS AND ENVIRONMENT ON 15N CHEMICAL SHIELDING ANISOTROPY IN PROTEINS. A COMBINATION OF DENSITY FUNCTIONAL THEORY, MOLECULAR DYNAMICS S IMULATION, AND NMR RELAXATION

S. F. Lienin, R. Brüschweiler, R. R. Ernst, 1999 .

Introducing color into stacking gels makes sample loading easy.

N. Skrynnikov, Yi Xue, Y. Ryabov, 2007, Analytical biochemistry.

Insights into Ubiquitin Product Release in Hydrolysis Catalyzed by the Bacterial Deubiquitinase SdeA.

C. Das, M. Wilson, N. Skrynnikov, 2021, Biochemistry.

Effect of rotation in NMR diffusion experiments on micron-sized particles: A generalized theoretical treatment.

N. Skrynnikov, I. S. Podkorytov, 2022, Journal of magnetic resonance.

Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD

Diego F. Gauto, I. Ayala, P. Schanda, 2022, bioRxiv.

Origin of anti-tumor activity of the cysteine-containing GO peptides and further optimization of their cytotoxic properties

O. Lyublinskaya, N. Skrynnikov, I. S. Podkorytov, 2017, Scientific Reports.

Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories

S. Saxena, S. A. Izmailov, N. Skrynnikov, 2020, Scientific Reports.

Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.

L. Kay, F. Dahlquist, N. Skrynnikov, 2002, Journal of the American Chemical Society.

A new structural arrangement in proteins involving lysine NH3+ group and carbonyl

L. Slipchenko, O. Rogacheva, S. A. Izmailov, 2017, Scientific Reports.

Efficient scalar spin relaxation in the rotating frame for matched radio-frequency fields

S. F. Lienin, R. Brüschweiler, R. R. Ernst, 1998 .

Proton-decoupled CPMG: a better experiment for measuring (15)N R2 relaxation in disordered proteins.

N. Skrynnikov, Tairan Yuwen, 2014, Journal of magnetic resonance.

Transient NOE-exchange-relay experiment: application to ligand-protein binding under slow exchange conditions.

N. Skrynnikov, I. S. Podkorytov, 2007, Journal of magnetic resonance.

15NH/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3

J. Forman-Kay, N. Skrynnikov, Yi Xue, 2010, Journal of Biomolecular NMR.

Very large residual dipolar couplings from deuterated ubiquitin

N. Skrynnikov, Nikolai R. Skrynnikov, Joshua M. Ward, 2012, Journal of Biomolecular NMR.

Very large residual dipolar couplings from deuterated ubiquitin

N. Skrynnikov, Joshua M. Ward, 2012, Journal of biomolecular NMR.

Deuterium spin probes of side-chain dynamics in proteins. 1. Measurement of five relaxation rates per deuteron in (13)C-labeled and fractionally (2)H-enriched proteins in solution.

L. Kay, D. Muhandiram, O. Millet, 2002, Journal of the American Chemical Society.

Observation of μs time-scale protein dynamics in the presence of Ln3+ ions: application to the N-terminal domain of cardiac troponin C

C. Eichmüller, N. Skrynnikov, 2007 .

Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?

C. Post, N. Skrynnikov, Tairan Yuwen, 2011, Journal of biomolecular NMR.

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.

N. Skrynnikov, Yi Xue, Tairan Yuwen, 2016, Biochemistry.

Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex.

J. Forman-Kay, V. Kanelis, D. Rotin, 2006, Structure.

Histone H4 tails in nucleosomes: a fuzzy interaction with DNA.

C. Jaroniec, M. Poirier, S. A. Izmailov, 2021, Angewandte Chemie.

Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin.

L. Kay, W. Choy, G. Mueller, 2000, Journal of molecular biology.

Observing the overall rocking motion of a protein in a crystal

Peixiang Ma, Yi Xue, Paul Schanda, 2015, Nature Communications.

Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics.

B. Reif, N. Skrynnikov, Yi Xue, 2010, Journal of the American Chemical Society.

Detection of nanosecond time scale side-chain jumps in a protein dissolved in water/glycerol solvent

N. Skrynnikov, Jun Xu, Yi Xue, 2009, Journal of biomolecular NMR.

Asymmetric doublets in MAS NMR: coherent and incoherent mechanisms

N. Skrynnikov, Nikolai R. Skrynnikov, 2007, Magnetic resonance in chemistry : MRC.

Domain orientation in β-cyclodextrin-loaded maltose binding protein: Diffusion anisotropy measurements confirm the results of a dipolar coupling study

L. Kay, P. Hwang, N. Skrynnikov, 2001, Journal of biomolecular NMR.

Relative Orientation of Peptide Planes in Proteins Is Reflected in Carbonyl-Carbonyl Chemical Shift Anisotropy Cross-Correlated Spin Relaxation

L. Kay, R. Konrat, D. Muhandiram, 2000 .

INTERMOLECULAR RELAXATION INVOLVING COUPLED SPIN SYSTEMS: A SIMPLIFIED APPROACH TO SOLVENT INDUCED RELAXATION

N. Skrynnikov, B. Sanctuary, T. N. Khazanovich, 1997 .

What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR.

L. Kay, F. Dahlquist, N. Skrynnikov, 2001, Journal of molecular biology.

Combined analysis of (15)N relaxation data from solid- and solution-state NMR spectroscopy.

B. Reif, A. Zhuravleva, N. Skrynnikov, 2007, Journal of the American Chemical Society.

Ensemble MD simulations restrained via crystallographic data: Accurate structure leads to accurate dynamics

N. Skrynnikov, Yi Xue, 2014, Protein science : a publication of the Protein Society.

Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions.

L. Kay, N. Skrynnikov, Ó. Millet, 2002, Journal of the American Chemical Society.

CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions

N. Skrynnikov, Tairan Yuwen, Tairan Yuwen, 2014, Journal of Biomolecular NMR.

CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions

N. Skrynnikov, Tairan Yuwen, 2014, Journal of biomolecular NMR.

High resolution 1H detected 1H,13C correlation spectra in MAS solid-state NMR using deuterated proteins with selective 1H,2H isotopic labeling of methyl groups.

B. Reif, A. Diehl, N. Skrynnikov, 2006, Journal of the American Chemical Society.

External Random Field Model for Intermolecular Spin Interactions: Accuracy Evaluation for the Coupled Relaxation of Two-Spin Molecules in a Pulse Responsive Solvent

N. Skrynnikov, T. N. Khazanovich, 1995 .

Orienting molecular fragments and molecules with residual dipolar couplings

N. Skrynnikov, 2004 .

Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings

L. Kay, N. Skrynnikov, L E Kay, 2000, Journal of biomolecular NMR.

Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43

D. Luzik, S. A. Izmailov, N. Skrynnikov, 2017, Scientific Reports.

Calculations of the contribution of ring currents to the chemical shielding anisotropy.

N. Skrynnikov, J. Boyd, 2002, Journal of the American Chemical Society.

A New Amide Proton R1ρ Experiment Permits Accurate Characterization of Microsecond Time-scale Conformational Exchange

C. Eichmüller, N. Skrynnikov, 2005, Journal of biomolecular NMR.

Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories

S. Saxena, S. A. Izmailov, N. Skrynnikov, 2020, Scientific Reports.

Measurement of Slow ( μ sms ) Time Scale Dynamics in Protein Side Chains by 15 N Relaxation Dispersion NMR Spectroscopy : Application to Asn and Gln Residues in a Cavity Mutant of T 4 Lysozyme

L. Kay, F. Dahlquist, F. Mulder, 2022 .

Correlation Spectra in MAS Solid-State NMR using Deuterated Proteins with Selective 1 H , 2 H Isotopic Labeling of Methyl Groups

B. Reif, A. Diehl, N. Skrynnikov, 2006 .

Microsecond time-scale dynamics from relaxation in the rotating frame: experiments using spin lock with alternating phase.

N. Skrynnikov, I. S. Podkorytov, 2004, Journal of magnetic resonance.

Comparison of 13 CH 3 , 13 CH 2 D, and 13 CHD 2<

L. Kay, V. Tugarinov, Jason E. Ollerenshaw, 2005 .

Combined Analysis of 15N Relaxation Data from Solid- and Solution-State NMR Spectroscopy

B. Reif, A. Zhuravleva, N. Skrynnikov, 2007 .

Detection of intermolecular chemical exchange through decorrelation of two-spin order.

R. R. Ernst, N. Skrynnikov, Nikolai R. Skrynnikov, 1999, Journal of magnetic resonance.

Geometric phase in NMR interferometry experiment

N. Skrynnikov, B. Sanctuary, 1994 .

The dynamics of strictly non-Volterra quadratic stochastic operators on the 2-simplex

Shengfan Zhou, Caidi Zhao, N. Skrynnikov, 2016 .