[Conformational stability of ribonuclease A complexes with specific inhibitors].
Isotermic unfolding of ribonuclease A, phosphopyridoxyl-8Lys41-RNAase A and complexes of the enzyme with cytidine, 2'-CMP, 3'-CMP, 3'-AMP and with the phosphoric ester of 1-(omega-oxypropyl)-cytosine in presence of urea has been studied. The stabilization of the protein structure resulting from the complex formation was shown to be determined by the ligand nucleobase binding. The comparison of the results obtained with those known from the literature suggests, that binding and catalytic zones of the enzyme active site form an integrated network system which is substained by multipoint contacts between the constituents. The change in the state of any part within the enzyme active state affects the energetics of the whole protein globule.
D000249:Adenosine Monophosphate; D001665:Binding Sites; D003562:Cytidine; D003568:Cytidine Monophosphate; D003596:Cytosine / Q000031:analogs & derivatives; D008239:Lysine; D008968:Molecular Conformation; D011732:Pyridoxal Phosphate; D012260:Ribonucleases / Q000037:antagonists & inhibitors*; D014508:Urea
D000249:Adenosine Monophosphate; D003562:Cytidine; D011732:Pyridoxal Phosphate; D003596:Cytosine; D014508:Urea; D012260:Ribonucleases; D003568:Cytidine Monophosphate; D008239:Lysine
Konformatsionnaia stabil'nost' kompleksov ribonukleazy A so spetsificheskimi ingibitorami.