Toward a proper interpretation of hydrogen exchange data in disordered proteins von Skrynnikov, Nikolai R.

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Slow conformational exchange and overall rocking motion in ubiquitin protein crystals von Kurauskas, Vilius, Izmailov, Sergei A., Rogacheva, Olga N., Hessel, Audrey, Ayala, Isabel, Woodhouse, Joyce, Shilova, Anastasya, Xue, Yi, Yuwen, Tairan, Coquelle, Nicolas, Colletier, Jacques-Philippe, Skrynnikov, Nikolai R., Schanda, Paul

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Slow Dynamics in Folded and Unfolded States of an SH3 Domain von Tollinger, Martin, Skrynnikov, Nikolai R, Mulder, Frans A. A, Forman-Kay, Julie D, Kay, Lewis E

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Order/Disorder Transitions Upon Protein Binding: A Unifying Perspective von Lebedenko, Olga O., Sekhar, Ashok, Skrynnikov, Nikolai R.

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Observing the overall rocking motion of a protein in a crystal von Ma, Peixiang, Xue, Yi, Coquelle, Nicolas, Haller, Jens D., Yuwen, Tairan, Ayala, Isabel, Mikhailovskii, Oleg, Willbold, Dieter, Colletier, Jacques-Philippe, Skrynnikov, Nikolai R., Schanda, Paul

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Effect of rotation in NMR diffusion experiments on micron-sized particles: A generalized theoretical treatment von Podkorytov, Ivan S., Skrynnikov, Nikolai R.

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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 Muta... von Yuwen, Tairan, Xue, Yi, Skrynnikov, Nikolai R

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Ensemble MD simulations restrained via crystallographic data: Accurate structure leads to accurate dynamics von Xue, Yi, Skrynnikov, Nikolai R.

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CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions von Yuwen, Tairan, Skrynnikov, Nikolai R.

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Modeling a unit cell: crystallographic refinement procedure using the biomolecular MD simulation platform Amber von Mikhailovskii, Oleg, Xue, Yi, Skrynnikov, Nikolai R

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X‑ray Crystallography Module in MD Simulation Program Amber 2023. Refining the Models of Protein Crystals von Mikhailovskii, Oleg, Izmailov, Sergei A., Xue, Yi, Case, David A., Skrynnikov, Nikolai R.

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Simulating diffraction photographs based on molecular dynamics trajectories of a protein crystal: a new option to examine structure-solving strategies in protein crystallography von Liu, Ning, Mikhailovskii, Oleg, Skrynnikov, Nikolai R, Xue, Yi

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Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy von Sun, Wenjun, Lebedenko, Olga O, Salguero, Nicole Gonzalez, Shannon, Matthew D, Zandian, Mohamad, Poirier, Michael G, Skrynnikov, Nikolai R, Jaroniec, Christopher P

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How Effective are Retro-Inverso Peptides? Insights from MD Supported by Paramagnetic NMR Data von Luzik, Dmitrii, Rogacheva, Olga, Skrynnikov, Nikolai

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Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43 von Rabdano, Sevastyan O., Izmailov, Sergei A., Luzik, Dmitrii A., Groves, Adam, Podkorytov, Ivan S., Skrynnikov, Nikolai R.

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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... von Xue, Yi, Yuwen, Tairan, Zhu, Fangqiang, Skrynnikov, Nikolai R

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Using NMR diffusion data to validate MD models of disordered proteins: Test case of N-terminal tail of histone H4 von Lebedenko, Olga O., Salikov, Vladislav A., Izmailov, Sergei A., Podkorytov, Ivan S., Skrynnikov, Nikolai R.

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Protein Side-Chain Dynamics As Observed by Solution- and Solid-State NMR Spectroscopy: A Similarity Revealed von Agarwal, Vipin, Xue, Yi, Reif, Bernd, Skrynnikov, Nikolai R

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Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data von Xue, Yi, Ward, Joshua M, Yuwen, Tairan, Podkorytov, Ivan S, Skrynnikov, Nikolai R

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Histone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA von Rabdano, Sevastyan O., Shannon, Matthew D., Izmailov, Sergei A., Gonzalez Salguero, Nicole, Zandian, Mohamad, Purusottam, Rudra N., Poirier, Michael G., Skrynnikov, Nikolai R., Jaroniec, Christopher P.

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