Thermodynamics

Complementary trimer binding to transfer‐RNAVal1

“…In the experiments, the tRNA concentration (50/aM) greatly exceeds the trimer concentration (5-50 nM). Therefore, the association constant K of a ttimer to a single complementary site on the tRNA molecule can be calculated by the relationship R = 1 + K [RNA], where R is the ratio of trimer counts in the chamber with the tRNA to the chamber without [7]. The experimental error in the evaluation of the association constants is estimated to be 20% for K-values above 10001/mole, and to be 50% for K-values below 1000 1/mole.…”

Complementary trimer binding to transfer RNAPhe

“…In the experiments, the tRNA concentration (40 PM) greatly exceeds the trimer concentration (5-50 nM). Therefore, the association constant K of a trimer to a single complementary site on the tRNA molecule can be calculated by the relationship R = 1 + K [RNA], where R is the ratio of trimer counts in the chamber with the tRNA to the chamber without [8]. The experimental error in the evaluation of the association constants is estimated to be 20% for K-values above 1000 l/mole, and to be 50% for K-values below 1000 l/mole.…”

Suppression of Insulin Aggregation by Heparin

“…42 Winzor, however, has pointed out the following limitations of this approach: (1) presumption of uniform charge distribution, (2) neglect of the effects of ion binding, and (3) assumption of identical accessibility and independent behavior of all ionizable groups. 43 For the present purposes, this approach facilitates quantitative visualization of the dipole-like nature of the charges on insulin.…”