Letters To The Editor
- In a recent article (1), the authors examine the binding of lab-evolved trans-activation response (TAR)–binding proteins (TBPs) to HIV-1 TAR RNA. Here, we show our analysis of the thermodynamic data of the binding that identifies three quantitative features of the binding, which may provide further insight into the interactions.where ΔH° and ΔS° are experimentally measured values reported in the original paper (1). Based on the statistical parameters, probability density of the ΔG° can be generated using Equation 2:where σ = 1.9407 kJ/mol and ΔG°mean = –41.3 kJ/mol.
- In a recent article (1), the authors examined biophysical characteristics in the interaction between methylated DNA and ZBTB38 protein, which possesses five zinc finger domains (ZFs 6–10) in the C-terminal region. While the authors identified that ZFs 6–9 were minimal structural elements for high-affinity DNA binding, the role of ZF 10 remained inconclusive. Here, we show that the binding data shown in Fig. 1 of the paper can be used to predict the role of ZF 10 in regard to binding to methylated DNA with an algebraic technique of solving a system of linear equations (2).
- We found a recent paper (1) that would be valuable in the field of protein thermodynamics. However, the paper contains some calculation errors. Here, we discuss the errors. Following the notations in Table 2 of the paper, the ensuing relationship of entropy can be established.