User profiles for N. R. Skrynnikov
Nikolai SkrynnikovSt. Petersburg State University / Purdue University Verified email at spbu.ru Cited by 9951 |
[BOOK][B] Amber 2021
Amber is the collective name for a suite of programs that allow users to carry out molecular
dynamics simulations, particularly on biomolecules. None of the individual programs carries …
dynamics simulations, particularly on biomolecules. None of the individual programs carries …
Slow dynamics in folded and unfolded states of an SH3 domain
15 N relaxation dispersion experiments were applied to the isolated N-terminal SH3 domain
of the Drosophila protein drk (drkN SH3) to study microsecond to second time scale …
of the Drosophila protein drk (drkN SH3) to study microsecond to second time scale …
Measurement of Slow (μs−ms) Time Scale Dynamics in Protein Side Chains by 15N Relaxation Dispersion NMR Spectroscopy: Application to Asn and Gln …
FAA Mulder, NR Skrynnikov, B Hon… - Journal of the …, 2001 - ACS Publications
A new NMR experiment is presented for the measurement of μs−ms time scale dynamics of
Asn and Gln side chains in proteins. Exchange contributions to the 15 N line widths of side …
Asn and Gln side chains in proteins. Exchange contributions to the 15 N line widths of side …
Reconstructing NMR spectra of “invisible” excited protein states using HSQC and HMQC experiments
NR Skrynnikov, FW Dahlquist… - Journal of the American …, 2002 - ACS Publications
Carr−Purcell−Meiboom−Gill (CPMG) relaxation measurements employing trains of 180
pulses with variable pulse spacing provide valuable information about systems undergoing …
pulses with variable pulse spacing provide valuable information about systems undergoing …
Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy
The use of a short, three-residue Cu 2+ -binding sequence, the ATCUN motif, is presented
as an approach for extracting long-range distance restraints from relaxation enhancement …
as an approach for extracting long-range distance restraints from relaxation enhancement …
Deuterium Spin Probes of Side-Chain Dynamics in Proteins. 1. Measurement of Five Relaxation Rates per Deuteron in 13C-Labeled and Fractionally 2H-Enriched …
…, DR Muhandiram, NR Skrynnikov… - Journal of the …, 2002 - ACS Publications
New pulse sequences are presented for the measurement of the relaxation of deuterium
double quantum, quadrupolar order, and transverse antiphase magnetization in 13 CH 2 D …
double quantum, quadrupolar order, and transverse antiphase magnetization in 13 CH 2 D …
Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: application to methionine residues in a …
NR Skrynnikov, FAA Mulder, B Hon… - Journal of the …, 2001 - ACS Publications
A relaxation dispersion-based NMR experiment is presented for the measurement and
quantitation of μs−ms dynamic processes at methyl side-chain positions in proteins. The …
quantitation of μs−ms dynamic processes at methyl side-chain positions in proteins. The …
An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates
DM Korzhnev, NR Skrynnikov, O Millet… - Journal of the …, 2002 - ACS Publications
Rotating-frame relaxation rates, R 1 ρ , are often measured in NMR studies of protein dynamics.
We show here that large systematic errors can be introduced into measured values of …
We show here that large systematic errors can be introduced into measured values of …
Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded …
Protein function is often regulated by conformational changes that occur in response to ligand
binding or covalent modification such as phosphorylation. In many multidomain proteins …
binding or covalent modification such as phosphorylation. In many multidomain proteins …
Deuterium spin probes of side-chain dynamics in proteins. 2. Spectral density mapping and identification of nanosecond time-scale side-chain motions
… Skrynnikov. Detection of nanosecond time scale side-chain jumps in a protein dissolved
in water/glycerol solvent. Journal of Biomolecular NMR 2009, 45 (1-2) , 57-72. …
in water/glycerol solvent. Journal of Biomolecular NMR 2009, 45 (1-2) , 57-72. …