Corrigendum to “Isothermal Titration Calorimetry and Surface Plasmon Resonance Analysis Using the Dynamic Approach”

The authors would like to sincerely apologize for some of the minor mistakes that have occurred in the development of the models, in particular, the equivalent conformation models meant for the sequential binding mechanism, detailed in the recently published article entitled "Isothermal Titration Calorimetry and Surface Plasmon Resonance Analysis Using the Dynamic Approach" (Biochemistry and Biophysics Reports, Volume 21, March 2020, 100712).In the published article, we have abstracted all the equivalent bound species and denoted them as a single species.Under such an assumption, the use of 'equivalent conformation factors' such as m, n becomes redundant and should be avoided.The justification for such changes is based on the fact that, for a given single site binding model, with M equivalent conformations, if we consider case such as (A) where m = 1 or (B) where, m = 10, the overall time profiles of its thermogram should not differ much (as shown below).Though the m values may differ, the total enthalpy associated with the binding process should be conserved.Similarly for a "M, N, two sets of equivalent binding sites with sequential binding", if we consider the case (A) where, m = 1 & n = 1, or case (B) where, m = 10 & n = 5, we obtain the following profiles.

Abstract licence: CC BY-NC

A person counts once a day per paper. We keep no cookie and no address: a reader is a hash that changes every day. Any month under five reads shows no number.