[Intermolecular interaction of adenosine-5'-phosphate with phenylalanine and tryptophan by nuclear magnetic resonance].
Equilibrium constants (K) of the complex formation of adenosine-5'-phosphate with phenylalanine (27 l/mol) and tryptophan (67 l/mol) in water (D2O, pD 9.9) have been determined. The comparison of the equilibrium constant values allowed to find the sequence of probabilities of the approach of aromatic amino acids to adenosine-5'-phosphate (tryptophan greater than tyrosine greater than phenylalanine). It has been shown that the dependence of lg K on l/T in the system phenylalanine-adenosine-5'-phosphate is non-linear. The ranges of the positive values of enthalpy (deltaH) and entropy (deltaS) changes of the complex phenylalanine-adenosine-5'-phosphate formation in the temperature interval 28-65 degrees have been found (deltaH = 0.2-1.5 kcal/mol, delta S = 14-50 e.u.). The conclusion about the hydrophobic interaction of aromatic cycles of nucleotide and amino acids has been deduced from the received data.
D000249:Adenosine Monophosphate; D002151:Calorimetry; D009682:Magnetic Resonance Spectroscopy; D010649:Phenylalanine; D013816:Thermodynamics; D014364:Tryptophan; D014443:Tyrosine
D000249:Adenosine Monophosphate; D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan
Issledovanie mezhmolekuliarnogo vzaimodeĭstviia adenozin-5'-fosfata s fenilalaninom i triptofanom metodom iadernogo magnitnogo rezonansa.