Thermodynamics of nucleotides binding to phosphorylase b

摘要: Abstract The effects of several chemical modifications in the AMP molecule on its interaction with phosphorylase b are examined by microcalorimetry, equilibrium dialysis, light scattering and ultracentrifuge experiments. In this work we report results obtained for eight analogues corresponding to different substituents puric base or ribose, positions phosphate. thermodynamic properties between above mentioned nucleotides also reported. following conclusions were obtained: a) Except IMP 2'dIMP all studied clearly show two types binding sites enzyme, b) nucleotide weaker affinity site is highly dependent upon alterations base. c) Both amino group C(6) N(1) adenine seem play an important role conformational transitions induced d) tetramerization presence 10 −2 M conditions experiments drastically affected ribose-phosphate part molecule.