Allostery involves coupling of conformational changes between two widely separated
binding sites. The common view holds that allosteric proteins are symmetric oligomers, with …

Cooperative effects in the binding of two or more substrates to different binding sites of a
receptor that are a result of a conformational change caused by the binding of the first …

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 …

Efficient determination of protein crystal structures requires automated x-ray data analysis.
Here, we describe the expert system elves and its use to determine automatically the …

The paper that introduced biochemists to the idea of allosteric feedback inhibition [Monod J,
Changeux J‐P & Jacob F (1963) J Mol Biol 6, 306–329] is now 50 years old, and the two …

The liganded hemoglobin (Hb) high-salt crystallization condition described by Max Perutz
has generated three different crystals of human adult carbonmonoxy hemoglobin (COHbA) …

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 …

< 1> Canis familiaris (isozymes A and B [1])[1]< 2> Rattus norvegicus (male rats [48];
Sprague-Dawley rats [40]; ST1A1 [40, 48]; AST IV [48]; aryl sulfotransferase IV [32, 48]; a …

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 …

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