Two fundamental principles can account for how regulated networks of interacting proteins
originated in cells. These are the law of mass action, which holds that the binding of one …

Assembly of hemoglobin subunits into cooperative complexes produces a remarkable
variety of architectures, ranging in oligomeric state from dimers to complexes containing 144 …

Many important proteins perform their physiological functions under allosteric control,
whereby the binding of a ligand at a specific site influences the binding affinity at a different …

An open question of great interest in biophysics is whether variations in structure cause
protein folds to differ in the number of amino acid sequences that can fold to them stably, ie …

Allostery is a property of biological macromolecules featuring cooperative ligand binding
and regulation of ligand affinity by effectors. The definition was introduced by Monod and …

Allosteric regulation of key metabolic enzymes is a fascinating field to study the structure-
function relationship of induced conformational changes of proteins. In this review we …

Allostery is an important regulatory phenomenon enabling precise control of biological
function. Initial understanding of allostery was gained from seminal work on conformational …

CAD, the multienzymatic protein that initiates and controls de novo synthesis of pyrimidines
in animals, associates through its aspartate transcarbamoylase (ATCase) domain into …

The allosteric enzyme aspartate transcarbamoylase (ATCase) from Escherichia coli has
been the subject of investigations for approximately 50years. This enzyme controls the rate …

Escherichia coli uses allantoin as the sole nitrogen source during anaerobic growth. In the
final step of allantoin degradation, oxamic transcarbamylase (OXTCase) converts oxalurate …