Understanding the function of biological macromolecules and their complexes at the
physicochemical level requires knowledge of both their structure and dynamics …

The structure of a protein complex together with information about its affinity and other
thermodynamic characteristics provide a “frozen” view of the complex. This picture ignores …

Proteins tendency to bind to one another in a highly specific manner forming stable
complexes is fundamental to all biological processes. A better understanding of complex …

Structural and mutational analyses reveal a central role for electrostatic interactions in
protein–protein association. Experiment and theory both demonstrate that clusters of …

WaterLOGSY represents a powerful method for primary NMR screening in the identification
of compounds interacting with macromolecules, including proteins and DNA or RNA …

Two types of noncovalent bonding interactions are present in protein structures, specific and
nonspecific. Nonspecific interactions are mostly hydrophobic and van der Waals. Specific …

Artificial endonucleases consisting of a Fok I cleavage domain tethered to engineered zinc-
finger DNA-binding proteins have proven useful for stimulating homologous recombination …

Kinetic data on a number of protein–protein associations have provided evidence for the
initial formation of a pre-equilibrium encounter complex that subsequently relaxes to the final …

Macromolecular complex formation is governed by two opposing constraints of specificity
and speed,. Kinetic,,, and theoretical considerations suggest that significant rate …

The structure of a protein–protein interaction, its affinity and thermodynamic characteristics
depict a 'frozen'state of a complex. This picture ignores the kinetic nature of complex …