Protein cross talking through osmotic work: the free energy of formation of the MgADP-myosin complexes at the muscle protein osmotic pressure

• Published in: Biochimica et biophysica acta Vol. 1388; no. 2; pp. 419 - 427
• Main Authors: Grazi, Enrico, Cuneo, Paola, Magri, Ermes, Adami, Raffaella, Trombetta, Giorgio
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 10.11.1998
• Subjects: Adenosine Diphosphate - analysis; Adenosine Diphosphate - chemistry; Animals; Chlorides - analysis; Formation energy; Muscle Contraction - physiology; Muscle protein; Muscle Proteins - chemistry; Muscle, Skeletal - physiology; Myosin-ADP complex; Myosins - chemistry; Osmotic Pressure; Protein Binding; Rabbits; Space life sciences; Thermodynamics; Water - chemistry; Formation energy; Myosin-ADP complex; Osmotic pressure; Muscle protein
• ISSN: 0167-4838; 0006-3002; 1879-2588
• DOI: 10.1016/S0167-4838(98)00198-8

A method is presented to determine the energy of formation of the myosin-ADP complexes at the muscle protein osmotic pressure. It is found that, at 18 kP, the putative protein osmotic pressure in skeletal muscle, the increase of MgADP from 0.05 to 2 mmolal, increases the free energy of myosin-ADP and of myosin-(ADP) 2 by 0.756 and by 9.85 kJ/mol, respectively, and decreases the free energy of myosin by 8.34 kJ erg/mol. It is pointed out that the local changes of water chemical potential, induced by the binding of MgADP to myosin, can be sensed by other structures of the contractile machinery, which per se may even be insensitive to MgADP. Cross talking between macromolecules can thus be achieved by changes of the water chemical potential.