Over the past 15 years there has been an explosion of research on the dynamical properties
of proteins, largely driven by the emergence of a handful of techniques that are sensitive to …

Au cours des dernières années, plusieurs nouvelles méthodes de RMN multidimensionnelle
ont été mises au point afin d'étudier la dynamique moléculaire au cours d'une longue …

The change in chemical shift (Δδ) observed for a given nucleus, when shifting from an
isotropic medium to a strongly oriented, liquid crystalline phase, contains valuable …

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

Two single cysteine substitution mutants at helix surface sites in T4 lysozyme (D72C and
V131C) have been modified with a series of nitroxide methanethiosulfonate reagents to …

NMR measurements of a large set of protein backbone one-bond dipolar couplings have
been carried out to refine the structure of the third IgG-binding domain of Protein G (GB3) …

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 …

1. Introduction 292. Landmarks in NMR of macromolecules 322.1 Protein structures and
methods development 322.1. 1 Sequential assignment method 322.1. 2 Triple-resonance …

The changes in a solute's chemical shifts between an isotropic and a liquid crystalline phase
provide information on the magnitude and orientation of the chemical shielding tensors …

The basic leucine zipper domain of the yeast transcription factor GCN4 consists of a C-
terminal leucine zipper and an N-terminal basic DNA-binding region that achieves a stable …