Kirillov S V, Odinzov V B
Nucleic Acids Res. 1978 May;5(5):1501-14. doi: 10.1093/nar/5.5.1501.
Earlier the existence of two conformers of Phe-tRNAPhe of E. coli was demonstrated because one of them yields complexes with 70S-poly(U) of extremely high affinity and the other with at least a 105 lower binding constant. We denote the first conformer as HAC (high affinity conformer) and the second as LAC (low affinity conformer). This high difference in binding constants was used for studying the process of reversible interconversion of conformers of Phe-tRNAPhe. The transition kinetics of LAC to HAC in conditions when the latter is stable (in the presence of magnesium ions) was studied and a high value of activation energy (35 kcal/mole) found. The interconversion is the first order reaction and equilibrium does not depend of overall Phe-tRNA concentration.
早些时候已证明大肠杆菌的苯丙氨酰 - tRNA苯丙氨酸存在两种构象异构体,因为其中一种能与70S - 聚(U)形成具有极高亲和力的复合物,而另一种的结合常数至少低105倍。我们将第一种构象异构体记为HAC(高亲和力构象异构体),第二种记为LAC(低亲和力构象异构体)。结合常数的这种巨大差异被用于研究苯丙氨酰 - tRNA苯丙氨酸构象异构体的可逆相互转化过程。研究了在后者稳定(存在镁离子)的条件下LAC向HAC的转变动力学,并发现了较高的活化能值(35千卡/摩尔)。这种相互转化是一级反应,且平衡不依赖于苯丙氨酰 - tRNA的总浓度。