Proteins are dynamic entities that undergo a plethora of conformational changes that may
take place on a wide range of time scales. These changes can be as small as the rotation of …

The mechanism of ligand binding coupled to conformational changes in macromolecules
has recently attracted considerable interest. The 2 limiting cases are the “induced fit” …

Allosteric interactions are typically considered to proceed through a series of discrete
changes in bonding interactions that alter the protein conformation. Here we show that …

Molecular recognition by proteins is fundamental to molecular biology. Dissection of the
thermodynamic energy terms governing protein–ligand interactions has proven difficult, with …

Allostery is a fundamental mechanism of regulation in biology. The residues at the end
points of long-range allosteric perturbations are commonly identified by the comparative …

To examine the relationship between protein structural dynamics and measurable hydrogen
exchange (HX) data, the detailed exchange behavior of most of the backbone amide …

Most proteins fold during biosynthesis on the ribosome, and co-translational folding
energetics, pathways and outcomes of many proteins have been found to differ considerably …

The cAMP-mediated allosteric transition in the catabolite activator protein (CAP; also known
as the cAMP receptor protein, CRP) is a textbook example of modulation of DNA-binding …

Membrane proteins are embedded in lipid bilayers and facilitate the communication
between the external environment and the interior of the cell. This communication is often …

Coarse-grained, self-contained polymer models are powerful tools in the study of protein
folding. They are also essential to assess predictions from less rigorous theoretical …