Allostery complex

The focus of this review article will be on the interaction between macromolecules and small-molecule ligands. The discussion will first center on the thermodynamic and kinetic characteristics that are used to measure the extent of binding. Subsequently, we discuss the interactions at the atomic level that drive complex formation. Then, a discussion follows of some tools available to predict macroscopic properties from microscopic properties. We then briefly discuss macromolec-ular motions as well as various aspects of receptor-ligand that have attracted renewed attention, such as conformational selection versus induced-fit, enthalpy-entropy compensation effect, and protein allostery. 

Advances in X-ray crystallography and nuclear magnetic resonance spectroscopy have facilitated the solution of a range of other allosteric proteins. These structures have contributed significantly to our understanding of the nature of allostery and the complex atomic level changes that accompany transitions from active/high affinity conformations to in-... 

This study and its predecessors have made at least modest inroads into the largely uncharted territory of the intricate interplay between static interactions and their dynamics in determining the stability of biologically active complexes. They have also raised a host of new questions, which remain to be answered before we could claim to understand the mechanisms of allostery and induced fit. Massive collection of data will be necessary to achieve this end. A correlation between the affinity (thermodynamic stability) and dynamic stability of a complex remains to be established - whether one considers intramolecular -intra- and interchain - complexes that hold the protein together, or the intermolecular complexes of a protein with its ligands. The atomic motions reflected in such processes as nuclear relaxation and backbone proton exchange -the main NMR indicators of protein dynamics remain to be described. Last, not... 

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