Nikolai R. Skrynnikov
Affiliations: | Chemistry | Purdue University, West Lafayette, IN, United States |
Area:
NMR is used to study proteins and nucleic acidsWebsite:
http://www.chem.purdue.edu/people/faculty/faculty.asp?itemID=60Google:
"Nikolai R. Skrynnikov"Bio:
http://www.chem.purdue.edu/skrynnikov/members.html
http://digitool.Library.McGill.CA:80/R/-?func=dbin-jump-full&object_id=34458&silo_library=GEN01
Parents
Sign in to add mentor| Bryan C. Sanctuary | grad student | 1996 | McGill | |
| (Effects of multispin modes in intermolecular NMR relaxation and chemical exchange in liquids) | ||||
| Richard R. Ernst | post-doc | 1997-1998 | ETH Zürich | |
| Lewis E. Kay | post-doc | 1999-2002 | University of Toronto | |
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Publications
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| Gauto DF, Lebedenko OO, Becker LM, et al. (2022) Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural Biology: X. 7: 100079 |
| Izmailov SA, Rabdano SO, Hasanbasri Z, et al. (2020) Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories. Scientific Reports. 10: 957 |
| Luzik DA, Rogacheva ON, Izmailov SA, et al. (2019) Molecular Dynamics model of peptide-protein conjugation: case study of covalent complex between Sos1 peptide and N-terminal SH3 domain from Grb2. Scientific Reports. 9: 20219 |
| Kämpf K, Izmailov SA, Rabdano SO, et al. (2018) What Drives N Spin Relaxation in Disordered Proteins? Combined NMR/MD Study of the H4 Histone Tail. Biophysical Journal. 115: 2348-2367 |
| Skrynnikov NR, Izmailov SA, Slipchenko LV, et al. (2018) Analysis of crystallographic structures and DFT calculations reveal a new structural arrangement in proteins involving lysine NH3 + group and carbonyl Acta Crystallographica Section a Foundations and Advances. 74: a175-a175 |
| Rogacheva ON, Izmailov SA, Slipchenko LV, et al. (2017) A new structural arrangement in proteins involving lysine NH3+ group and carbonyl. Scientific Reports. 7: 16402 |
| Kurauskas V, Izmailov SA, Rogacheva ON, et al. (2017) Slow conformational exchange and overall rocking motion in ubiquitin protein crystals. Nature Communications. 8: 145 |
| Yuwen T, Xue Y, Skrynnikov NR. (2016) 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 |
| Izmailov SA, Podkorytov IS, Skrynnikov NR. (2016) MD Modeling of Oxidative Folding in Peptides and Proteins Biophysical Journal. 110: 644a-645a |
| Ma P, Xue Y, Coquelle N, et al. (2015) Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6: 8361 |