Dubey, Abhinav Takeuchi, Koh Reibarkh, Mikhail Arthanari, Haribabu
Published in
Journal of Biomolecular NMR
Nuclear magnetic resonance (NMR) spectroscopy has contributed to structure-based drug development (SBDD) in a unique way compared to the other biophysical methods. The potency of a ligand binding to a protein is dictated by the binding free energy, which is an intricate interplay between entropy and enthalpy. In addition to providing the atomic res...
Norton, Raymond S. Jahnke, Wolfgang
Published in
Journal of Biomolecular NMR
Overbeck, Jan H. Kremer, Werner Sprangers, Remco
Published in
Journal of Biomolecular NMR
AbstractProteins and nucleic acids are highly dynamic bio-molecules that can populate a variety of conformational states. NMR relaxation dispersion (RD) methods are uniquely suited to quantify the associated kinetic and thermodynamic parameters. Here, we present a consistent suite of 19F-based CPMG, on-resonance R1ρ and off-resonance R1ρ RD experim...
Vugmeyster, Liliya Perazzolo, Chiara Wist, Julien Frueh, Dominique Bodenhausen, Geoffrey
Published in
Journal of Biomolecular NMR
Cross-correlated fluctuations of isotropic chemical shifts can provide evidence for slow motions in biomolecules. Slow side-chain dynamics have been investigated in 15N and 13C enriched ubiquitin by monitoring the relaxation of Cα-Cβ two-spin coherences (Frueh et al., 2001). This method, which had hitherto been demonstrated only for protonated ubiq...
Dittmer, Jens Kim, Chul-Hyun Bodenhausen, Geoffrey
Published in
Journal of Biomolecular NMR
The bond lengths and dynamics of intra- and intermolecular hydrogen bonds in an RNA kissing complex have been characterized by determining the NMR relaxation rates of various double- and triple-quantum coherences that involve an imino proton and two neighboring nitrogen-15 nuclei belonging to opposite bases. New experiments allow one to determine t...
Cutting, Brian Tolman, Joel R. Nanchen, Steve Bodenhausen, Geoffrey
Published in
Journal of Biomolecular NMR
The determination of residual dipolar couplings (RDCs) by quantitative J spectroscopy methods such as Heteronuclear Single Quantum Correlation with Phase Encoded Coupling (HSQC-PEC) is prone to systematic errors that may be caused by differential attenuation during the conversion of orthogonal density operator components into observable terms. The ...
Simon, Bernd Köstler, Herbert
Published in
Journal of Biomolecular NMR
Apodization weighted acquisition is a simple approach to enhance the sensitivity of multidimensional NMR spectra by scaling the number of scans during acquisition of the indirect dimension(s). The signal content of the resulting spectra is identical to conventionally sampled data, yet the spectra show improved signal-to-noise ratios. There are no s...
DeLisle, Charles F. Mendis, H. Bhagya Lorieau, Justin L.
Published in
Journal of Biomolecular NMR
Spectral resolution remains one of the most significant limitations in the NMR study of biomolecules. We present the srNOESY (super resolution nuclear overhauser effect spectroscopy) experiment, which enhances the resolution of NOESY cross-peaks at the expense of the diagonal peak line-width. We studied two proteins, ubiquitin and the influenza hem...
Williams, Robert V. Yang, Jeong-Yeh Moremen, Kelley W. Amster, I. Jonathan Prestegard, James H.
Published in
Journal of Biomolecular NMR
Residual dipolar couplings (RDCs) provide both structural and dynamical information useful in the characterization of biological macromolecules. While most data come from the interaction of simple pairs of directly bonded spin-1/2 nuclei (1H–15N, 1H–13C, 1H–1H), it is possible to acquire data from interactions among the multiple spins of 13C-labele...
Tripsianes, Konstantinos Schütz, Ulrike Emmanouilidis, Leonidas Gemmecker, Gerd Sattler, Michael
Published in
Journal of Biomolecular NMR
The physiological role of proteins is frequently linked to interactions with non-protein ligands or posttranslational modifications. Structural characterization of these complexes or modified proteins by NMR may be difficult as the ligands are usually not available in an isotope-labeled form and NMR spectra may suffer from signal overlap. Here, we ...