The 'EF-hand'Ca2+-binding motif plays an essential role in eukaryotic cellular signalling,
and the proteins containing this motif constitute a large and functionally diverse family. The …

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

We used nuclear magnetic resonance relaxation dispersion to characterize higher energy
conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in …

Nuclear-magnetic-resonance spectroscopy can determine the three-dimensional structure of
proteins in solution. However, its potential has been limited by the difficulty of interpreting …

The calcium binding proteins of the EF-hand super-family are involved in the regulation of all
aspects of cell function. These proteins exhibit a great diversity of composition, structure …

Time-dependent dynamical properties of molecules can be quantified with atomic resolution
by using solution-state NMR spectroscopy. A variety of NMR observables, including scalar …

EF-hand calcium binding proteins have remarkable sequence homology and structural
similarity, yet their response to binding of calcium is diverse and they function in a wide …

The DSSP program assigns protein secondary structure to one of eight states. This discrete
assignment cannot describe the continuum of thermal fluctuations. Hence, a continuous …

Conformational changes occurring on the microsecond− millisecond time scale in basic
pancreatic trypsin inhibitor (BPTI) are investigated using nuclear magnetic resonance …

The versatile optical and biological properties of a localized surface plasmon resonance
(LSPR) sensor that responds to protein conformational changes are illustrated. The sensor …