The eukaryotic cell is a bustling collection of macromolecules acting cooperatively to
mediate the functions required for cell viability. Specific, context-dependent and tightly …

A significant fraction of every proteome is occupied by biologically active proteins that do not
form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and …

Abstract Src homology 3 (SH3) domains are involved in the regulation of important cellular
pathways, such as cell proliferation, migration and cytoskeletal modifications. Recognition of …

Allostery, the process by which distant sites within a protein system are energetically
coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely …

The kinesin-3 family is one of the largest among the kinesin superfamily and its members
play important roles in a wide range of cellular transport activities, yet the molecular …

Cis-peptide bonds are rare in proteins, and building blocks less favorable to the trans-
conformer have been considered destabilizing. Although proline tolerates the cis-conformer …

Protein conformational switches alter their shape upon receiving an input signal, such as
ligand binding, chemical modification, or change in environment. The apparent simplicity of …

The cytosolic fraction of the tumor suppressor p53 activates the apoptotic effector protein
BAX to trigger apoptosis. Here we report that p53 activates BAX through a mechanism …

Protein kinase A (PKA) is a prototype of multidomain signaling proteins functioning as
allosteric conformational switches. Allosteric transitions have been the subject of extensive …

Prolyl isomerizations are intrinsically slow processes. They determine the rates of many
protein folding reactions and control regulatory events in folded proteins. Prolyl isomerases …