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Nikolai R. Skrynnikov

Nikolai R.  Skrynnikov Profile Picture

Assistant Professor — Chemistry
Ph.D. 1996 McGill University


Contact Info:

nskrynni@purdue.edu
765-494-8519


Training Group(s):
Biomolecular Structure and Biophysics


Current Research Interests:

Nuclear Magnetic Resonance (NMR) is one of the most powerful and versatile techniques used for the characterization of biomolecules. Notably, NMR is used to study proteins and nucleic acids under conditions that are reasonably close to those found inside living cells, achieving nearly complete structural and dynamic characterization of the molecules. Short of complete characterization, a number of important questions can be answered with purposefully designed NMR experiments.Our research involves the development and application of NMR techniques with the focus on complex forms of molecular motion, such as slow time-scale (µs-ms) protein dynamics, dynamics of unfolded and partially folded proteins, and dynamics involved in protein-ligand interactions. These forms of motion often hold the key to the efficiency and timing of enzymatic catalysis, signal transduction, and other biological processes of critical importance. Our research involves a broad range of tasks beginning with bacterial expression and purification of proteins and, prominently, the design, implementation, and execution of multidimensional heteronuclear NMR experiments. On the theoretical side, the projects are supported by the spin density matrix calculations, molecular dynamics and density functional theory computations.



Selected Publications:

Xu J., Millet O., Kay L.E., Skrynnikov N.R. "A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups", J. Am. Chem. Soc., in press (2005).

Skrynnikov N.R., Dahlquist F.W., Kay L.E., "Reconstructing NMR spectra of 'invisible' excited protein states using HSQC and HMQC experiments", J. Am. Chem. Soc. 124 (41):12352 - 12360 (2002).

Skrynnikov N.R., Goto N.K., Yang D.W., Choy W.Y., Tolman J.R., Mueller G.A., Kay L.E., "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", J. Mol. Biol. 295 (5):1265-1273 (2000).

Skrynnikov N.R., Ernst R.R., "Detection of intermolecular chemical exchange through decorrelation of two-spin order", J. Magn. Reson. 137 (1):276-280 (1999).

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