In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Binding events of ligands to receptors are the key for an understanding of biological
processes. Gaining insight into protein–protein and protein–ligand interactions in solution …

A comparison of HSQC and HMQC pulse schemes for recording 1H− 13C correlation maps
of protonated methyl groups in highly deuterated proteins is presented. It is shown that …

A major goal in structural biology is to unravel how molecular machines function in detail. To
that end, solution-state NMR spectroscopy is ideally suited as it is able to study biological …

The development of isotope labeling methodology has had a significant impact on NMR
studies of high-molecular-weight proteins and macromolecular complexes. Here we review …

▪ Abstract During the past thirty years, deuterium labeling has been used to improve the
resolution and sensitivity of protein NMR spectra used in a wide variety of applications. Most …

A selective protonation strategy is described that uses [3-2H] 13C α-ketoisovalerate to
introduce (1H-δ methyl)-leucine and (1H-γ methyl)-valine into 15N-, 13C-, 2H-labeled …

Internuclear distances represent one of the main structural constraints in molecular structure
determination using solid-state NMR spectroscopy, complementing chemical shifts and …

New NMR experiments are presented for the assignment of methyl 13C and 1H chemical
shifts from Ile, Leu, and Val residues in high molecular weight proteins. The first class of …

The interaction between leukocyte function-associated antigen-1 (LFA-1) and intracellular
adhesion molecule-1 (ICAM-1) has been implicated in inflammatory and immune diseases …