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 …

Molecular dynamics simulations capture the behavior of biological macromolecules in full
atomic detail, but their computational demands, combined with the challenge of …

Proteins often undergo large conformational changes when binding small molecules, but
atomic-level descriptions of such events have been elusive. Here, we report unguided …

INTRODUCTION Protein kinases mediate many cell signaling processes. Central to their
physiological function is the regulation of their binding and enzymatic activities, which is …

The detailed understanding of the binding of small molecules to proteins is the key for the
development of novel drugs or to increase the acceptance of substrates by enzymes …

Eukayotic protein kinases evolved as a family of highly dynamic molecules with strictly
organized internal architecture. A single hydrophobic F-helix serves as a central scaffold for …

The ATP site of kinases displays remarkable conformational flexibility when accommodating
chemically diverse small molecule inhibitors. The so-called activation segment, whose …

Although the thermodynamic principles that control the binding of drug molecules to their
protein targets are well understood, detailed experimental characterization of the process by …

Molecular dynamics simulations allow for atomic-level characterization of biomolecular
processes such as the conformational transitions associated with protein function. The …

Unregulated activation of Src kinases leads to aberrant signalling, uncontrolled growth and
differentiation of cancerous cells. Reaching a complete mechanistic understanding of large …