This review focuses upon the application of solution NMR methods to multispan integral
membrane proteins, particularly with respect to determination of global folds by this …

Solution NMR studies of biomolecules are typically limited by the molecules' molecular
weight. Here we report strategies based on the use of highly deuterated, methyl‐protonated …

The size of proteins that can be studied by solution NMR spectroscopy has increased
significantly because of recent developments in methodology. Important experiments …

The NMR determination of the structure of large biological macromolecules in solution is
primarily limited by the fast transverse relaxation that broadens lines and reduces spectral …

In the past decade, residual dipolar couplings (RDCs) have revolutionized biomolecular
nuclear magnetic resonance spectroscopy. Recent developments indicate that this …

A strategy for the introduction of (1 H, 13 C-methyl)-alanine into perdeuterated proteins is
described. Specific protonation of alanine methyl groups to a level of 95% can be achieved …

Residual dipolar couplings (RDCs) have already revolutionized biomolecular NMR
spectroscopy and are about to do the same in small molecule applications: impressive …

Achieving homonuclear 1H decoupling remains one of the key challenges in liquid-state
NMR. Such spectra would endow a variety of organic and analytical applications with an …

Roughly one-third of all proteins reside in biological membranes [1, 2]. Integral membrane
proteins (IMPs), which can only be released from the membrane by disruption of the …

NMR has matured into a technique routinely employed for studying proteins in near
physiological conditions. However, applications to larger proteins are impeded by the …