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 ...
Bergonzo, Christina Grishaev, Alexander
Published in
Journal of Biomolecular NMR
Structural information about ribonucleic acid (RNA) is lagging behind that of proteins, in part due to its high charge and conformational variability. Molecular dynamics (MD) has played an important role in describing RNA structure, complementing information from both nuclear magnetic resonance (NMR), or X-ray crystallography. We examine the impact...
Matviychuk, Yevgen Bostock, Mark J. Nietlispach, Daniel Holland, Daniel J.
Published in
Journal of Biomolecular NMR
We present a model-based method for estimation of relaxation parameters from time-domain NMR data specifically suitable for processing data in popular 2D phase-sensitive experiments. Our model is formulated in terms of commutative bicomplex algebra, which allows us to use the complete information available in an NMR signal acquired with principles ...
Christensen, Malene V. Kongstad, Kenneth T. Sondergaard, Teis Esben Staerk, Dan Nielsen, Hanne M. Franzyk, Henrik Wimmer, Reinhard
Published in
Journal of Biomolecular NMR
Current methods for assessment of cellular uptake of cell-penetrating peptides (CPPs) often rely on detection of fluorophore-labeled CPPs. However, introduction of the fluorescent probe often confers changed physicochemical properties, so that the fluorophore-CPP conjugate may exhibit cytotoxic effects and membrane damage not exerted by the native ...
