Cytidine 2’-monophosphate, ribonuclease

Gorenstein, D. G., Wywicz, A. M. and Bode, J. (1976) Interaction of Uridine and Cytidine Monophosphates with Ribonuclease A. IV Phosphorus-31 Nuclear Magnetic Resonance Studies, J. Am. Chem. Soc. 98,2308. 

There are now well over 200 publications in which microcalorimetry has specifically been used to study protein-hgand interactions of a variety of types. A fist of these studies is readily available by a MEDLINE search or from ITC equipment suppliers. Since the studies are too numerous to review here, perhaps a recent one might serve as a representative example of the technique and of its application. In this example [40] we determined the thermodynamic parameters associated with the binding of the reversible inhibitor 2 -CMP (2 -cytidine monophosphate) to RNAse-A (ribonuclease A). We were specifically interested in the binding under conditions that were relatively physiological, i.e., at body temperature and in a buffer that contained multiple ions at roughly cellular concentrations. 

The binding affinity of a ligand to a protein. Figure 27.18 shows the binding constant K for binding cytidine monophosphate to ribonuclease A, as a function of l/T where T is temperature. For T = 300 K, compute... 

Cy tidy lie Acid. Cyridine-3 -monophosphate cytidylic acid b 3 -cytidinephosphoric acid cytidine-3 -phosphate 3 -cytosylic acid 3 -CMP, CjH NjOjP mol wt 323.19. C 33.44% H 4-37%, N 13.00%, O 39-61%. P 9 58% Ribonuclease inhibitor. Prepn from yeast ribonucleic acid see refs under 2 -Cytidylic Acid. Prepn by pancreatic-ribonuclease-catalyzed ring opening of dicyclohexy] -guanidinium cytidine 2 ,3 -cyclic phosphate Lohrmann,... 

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