Nikolai R. Skrynnikov

Affiliations: 
Chemistry Purdue University, West Lafayette, IN, United States 
Area:
NMR is used to study proteins and nucleic acids
Website:
http://www.chem.purdue.edu/people/faculty/faculty.asp?itemID=60
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"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

Mean distance: 9.3
 
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Parents

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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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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
Ma P, Xue Y, Coquelle N, et al. (2015) Observing the overall rocking motion of a protein in a crystal. Nature Communications. 6: 8361
Skrynnikov NR, Tycko R. (2015) Interview with Robert Tycko: On amyloids, Alzheimer disease, and solid-state NMR Concepts in Magnetic Resonance Part a: Bridging Education and Research. 44: 182-189
Xue Y, Yuwen T, Zhu F, et al. (2014) 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. 53: 6473-95
Yuwen T, Skrynnikov NR. (2014) CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions. Journal of Biomolecular Nmr. 58: 175-92
Xue Y, Skrynnikov NR. (2014) Ensemble MD simulations restrained via crystallographic data: accurate structure leads to accurate dynamics. Protein Science : a Publication of the Protein Society. 23: 488-507
Yuwen T, Skrynnikov NR. (2014) Proton-decoupled CPMG: a better experiment for measuring (15)N R2 relaxation in disordered proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 155-69
Ward JM, Skrynnikov NR. (2012) Very large residual dipolar couplings from deuterated ubiquitin. Journal of Biomolecular Nmr. 54: 53-67
Xue Y, Ward JM, Yuwen T, et al. (2012) Microsecond time-scale conformational exchange in proteins: using long molecular dynamics trajectory to simulate NMR relaxation dispersion data. Journal of the American Chemical Society. 134: 2555-62
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