• Corpus ID: 216562764

Hadamard magnetization transfers achieve dramatic sensitivity enhancements in homonuclear multidimensional NMR correlations of labile sites in proteins, polysaccharides and nucleic acids

  title={Hadamard magnetization transfers achieve dramatic sensitivity enhancements in homonuclear multidimensional NMR correlations of labile sites in proteins, polysaccharides and nucleic acids},
  author={Mihajlo Novakovic and E Riks Kup{\vc}e and Andreas Oxenfarth and Marcos D. Battistel and Dar{\'o}n I. Freedberg and Harald Schwalbe and Lucio Frydman Department of Chemical and Biological Physics and Weizmann Institute of Science and Rehovot and Israel Bruker UK Ltd. and Coventry and UK Center for Biomolecular Magnetic Resonance and Johann Wolfgang Goethe-University and FrankfurtMain and Germany Center for Biologics Evaluation and Research and Food and Drug Administration and Silver Spring and Maryland. and United States},
  journal={arXiv: Chemical Physics},
EXSY, TOCSY and NOESY lie at the foundation of homonuclear NMR experiments in organic and pharmaceutical chemistry, as well as in structural biology. Limited magnetization transfer efficiency is an intrinsic downside of these methods, particularly when targeting rapidly exchanging species such as labile protons ubiquitous in polysaccharides, sidechains and backbones of proteins, and in bases and sugars of nucleic acids: the fast decoherence imparted on these protons through solvent exchanges… 

Figures from this paper

Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics

The application of methods for signal-to-noise increases, including dynamic nuclear polarisation, hyperpolarisation and photo-CIDNP for the study of time-resolved NMR studies are discussed.

The robust NMR toolbox for metabolomics.

A suite of selective and non-selective CPMG-filtered 1D and 2D TOCSY/HSQC experiments for metabolomics research facilitated the unambiguous identification of metabolites embedded in broad lipid and protein signals.



Heteronuclear 1D and 2D NMR Resonances Detected by Chemical Exchange Saturation Transfer to Water.

A method to detect NMR spectra from heteronuclei through the modulation that they impose on a water resonance is exemplified and enables 2D heteronuclear acquisitions on directly bonded 1 H-15 N spin pairs with significant signal amplification.

Sensitivity-enhanced detection of non-labile proton and carbon NMR spectra on water resonances.

The present study expands CEST principles by fusing into these experiments homonuclear isotropic mixing sequences, enabling the water-enhanced detection of non-exchangeable species, and becomes a sensitive alternative to detect non- exchangeable species in biomolecules.

Rapid heteronuclear single quantum correlation NMR spectra at natural abundance.

A novel NMR experiment, the so-called ASAP-HSQC, is introduced that allows the detection of heteronuclear one-bond correlations in less than 30 s on small molecules at natural abundance without

Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation

It is demonstrated, by means of experiments with the basic pancreatic trypsin inhibitor, that the buildup rates of the nuclear Overhauser effect can be measured by two-dimensional NMR spectroscopy.

SOFAST-HMQC Experiments for Recording Two-dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds

This work investigates in detail the performance of SOFAST-HMQC to record 1H–15N and 1H−13C correlation spectra of proteins of different size and at different magnetic field strengths.

CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions

The experiment termed CP-HISQC (cross-polarization assisted heteronuclear in-phase single-quantum correlation) is implemented, which demonstrates that proton-to-nitrogen CP transfer remains highly efficient in the presence of solvent exchange as fast as kex = 620 s−1, and offers much better spectral resolution than conventional HSQC-type experiments.