Proton-selective 17O-1H distance measurements in fast magic-angle-spinning solid-state NMR spectroscopy for the determination of hydrogen bond lengths.

Supporting Information: Proton-Selective 17O–1H Distance Measurements in Fast Magic-Angle-Spinning Solid-State NMR Spectroscopy for the Determination of Hydrogen Bond Lengths

Sensitivity enhancement and heteronuclear distance measurements in biological 17O solid-state NMR.

In this contribution we present a comprehensive approach to study hydrogen bonding in biological and biomimetic systems through 17O and 17O-1H solid-state NMR combined with density functional theory calculations of 17O and 1H NMR parameters. We explore the signal enhancement of 17O in L-tyrosine.HCl using repetitive double-frequency swept radio frequency pulses in solid-state NMR. The technique...

An investigation of the hydrogen-bonding structure in bilirubin by 1H double-quantum magic-angle spinning solid-state NMR spectroscopy.

The complex hydrogen-bonding arrangement in the biologically important molecule bilirubin IXalpha is probed by using 1H double-quantum (DQ) magic-angle spinning (MAS) NMR spectroscopy. Employing fast MAS (30 kHz) and a high magnetic field (16.4 T), three low-field resonances corresponding to the different hydrogen-bonding protons are resolved in a 1H MAS NMR spectrum of bilirubin. These resonan...

Proton chemical shift anisotropy measurements of hydrogen-bonded functional groups by fast magic-angle spinning solid-state NMR spectroscopy.

The suitability of fast MAS solid-state NMR spectroscopy for probing (1)H chemical shift anisotropy of hydrogen-bonded species has been demonstrated.

Selective 1H-1H Distance Restraints in Fully Protonated Proteins by Very Fast Magic-Angle Spinning Solid-State NMR.

Very fast magic-angle spinning (MAS > 80 kHz) NMR combined with high-field magnets has enabled the acquisition of proton-detected spectra in fully protonated solid samples with sufficient resolution and sensitivity. One of the primary challenges in structure determination of protein is observing long-range 1H-1H contacts. Here we use band-selective spin-lock pulses to obtain selective 1H-1H con...