Function in biological systems is exquisitely dependent on spatial and temporal changes in
biomacromolecules. Innumerable biological processes ultimately rely on transduction of …

The use of residual dipolar couplings (RDCs) in the analysis of biomolecular structure and
dynamics has expanded rapidly since its potential as a source of structural information on …

Protein structure is inherently dynamic, with function often predicated on excursions from low
to higher energy conformations. For example, X-ray studies of a cavity mutant of T4 …

Protein solution nuclear magnetic resonance (NMR) can be conducted in a slightly
anisotropic environment, where the orientational distribution of the proteins is no longer …

The solution structure of Ca2+-ligated calmodulin is determined from residual dipolar
couplings measured in a liquid crystalline medium and from a large number of …

Since the first applications of residual dipolar couplings (RDCs) to biomolecular systems
approximately a decade ago, RDCs have rapidly emerged as a standard tool for the …

An overview is presented of some of the major insights that have come from studies of the
structure, stability, and folding of T4 phage lysozyme. A major purpose of this review is to …

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 …

Compressed and stretched polyacrylamide hydrogels previously have been shown to offer a
robust method for aligning proteins. A simple, funnel-like apparatus is described for …

▪ Abstract Residual dipolar couplings (RDCs) have recently emerged as a new tool in
nuclear magnetic resonance (NMR) with which to study macromolecular structure and …