▪ Abstract NMR spin relaxation spectroscopy is a powerful approach for characterizing
intramolecular and overall rotational motions in proteins. This review describes experimental …

Nuclear magnetic resonance (NMR) spectroscopy is now established as the method of
choice for the study of the structure and dynamics of proteins and nucleic acids in solution …

Carbon-13 chemical shift anisotropy (CSA) tensors for various carbon sites of polypeptides,
and for carbon sites in α-helical and β-sheet conformations of poly-l-alanine, and …

The principal components and orientations of the chemical shift anisotropy (CSA) tensors of
the carbonyl (C '), nitrogen (N), and amide proton (HN) nuclei of 64 distinct amide bonds in …

A series of experiments are presented that provide an exchange-free measure of dipole−
dipole 15N transverse relaxation, R dd, that can then be substituted for 15N R 1ρ or R 2 …

The NMR spin–lattice relaxation rate (R1) and the rotating-frame spin–lattice relaxation rate
(R1ρ) of amide 15N and carbonyl 13C (13C′) of the uniformly 13C-and 15N-labeled …

A new strategy has been developed to measure cross-correlation rates with much enhanced
accuracy. The method relies on the use of four complementary experiments. Errors due to …

Structure calculations of proteins, oligonucleotides, and other molecules of biological
interest rely on the measurement of proton–proton distances from nuclear Overhauser effect …

The effect of small amplitude anisotropic peptide plane motion on residual dipolar couplings
(RDC) measured in proteins has been investigated. RDC averaging effects in the presence …

New nuclear magnetic resonance (NMR) methods are described for the measurement of
cross-correlation rates of zero-and double-quantum coherences involving two nitrogen …