Literature DB >> 26477875

Optimizing isothermal titration calorimetry protocols for the study of 1:1 binding: Keeping it simple.

Joel Tellinghuisen1.   

Abstract

BACKGROUND: Successful ITC experiments require conversion of cell reagent (titrand M) to product and production or consumption of heat. These conditions are quantified for 1:1 binding, M+X ⇔ MX.
METHODS: Nonlinear least squares is used in error-propagation mode to predict the precisions with which the key quantities - binding constant K, reaction enthalpy ΔH°, and stoichiometry number n - can be estimated over a wide range of the dimensionless quantity that governs isotherm shape, c=K[M]0. The measurement precision σq is estimated from analysis of water-water blanks.
RESULTS: When the product conversion exceeds 90%, the parameter relative standard errors are proportional to σq/qtot, where the total heat qtot ≈ ΔH° [M]0V0. Specifically, σK/K×qtot/σq ≈ 25 for c=10(-3)-10, ≈ 11 c(1/3) for c=10-10(4). For c>1, n and ΔH° are more precise than K; this holds also at smaller c for the product n×ΔH° and for ΔH° when n can be held fixed. Use of as few as 10 titrant injections can outperform the customary 20-40 while also improving productivity.
CONCLUSION: These principles are illustrated in experiment design using the program ITC-PLANNER15. GENERAL SIGNIFICANCE: Simple quantitative guidelines replace the "c rules" that have dominated the literature for decades.
Copyright © 2015 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Data analysis; Experiment design; ITC; Nonlinear least squares; Statistical errors

Mesh:

Substances:

Year:  2015        PMID: 26477875     DOI: 10.1016/j.bbagen.2015.10.011

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


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