Probing Solution Thermodynamics by Microcalorimetry

Poon, Gregory M.K.

doi:10.5772/19549

Cited by 2 publications

(1 citation statement)

References 30 publications

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“…Titrations were performed by injecting DNA into protein in a Nano ITC instrument (TA Instruments). Model-dependent analysis was performed as described (27,28). For PU.1, which undergoes self-dimerization in both DNA-free and -bound states at high concentrations (Ͼ10 Ϫ5 M), we followed our previously described model to extract the enthalpy changes for the canonical 1:1 complex (29).…”

Section: Methodsmentioning

confidence: 99%

Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-binding Domains of the ETS Family Transcription Factors Ets-1 and PU.1

Wang

Linde

Munde

et al. 2014

Journal of Biological Chemistry

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Background: ETS family transcription factors recognize DNA via structurally conserved DNA-binding domains that share limited amino acid homology. Results: DNA recognition by the ETS domains of Ets-1 and PU.1, two extreme sequence-divergent paralogs, was compared. Conclusion: Preferential hydration differentiates DNA recognition by Ets-1 and PU.1. Significance: Preferential hydration represents a potential mechanism for PU.1 regulation and its activity as a pioneer transcription factor in vivo.

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Section: Methodsmentioning

confidence: 99%

Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-binding Domains of the ETS Family Transcription Factors Ets-1 and PU.1

Wang

Linde

Munde

et al. 2014

Journal of Biological Chemistry

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ITC and SPR Analysis Using Dynamic Approach

Krishnamoorthy¹,

Krishanmoorthy

Alluvada

et al. 2019

Preprint

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Biophysical techniques such as Isothermal Calorimetry (ITC) and Surface Plasmon Resonance (SPR) are routinely used to ascertain the global binding mechanisms of protein-protein or protein-ligand interaction. Recently, Dumas etal, have explicitly modelled the instrument response of the ligand dilution and analysed the ITC thermogram to obtain kinetic rate constants.Adopting a similar approach, we have integrated the dynamic instrument response with the binding mechanism to simulate the ITC profiles of equivalent and independent binding sites, equivalent and sequential binding sites and aggregating systems. The results were benchmarked against the standard commercial software Origin-ITC. Further, the experimental ITC chromatograms of 2'-CMP + RNASE and BH3I-1 + hBCL XL interactions were analysed and shown to be comparable with that of the conventional analysis. Dynamic approach was applied to simulate the SPR profiles of a two-state model, and could reproduce the experimental profile accurately.

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Probing Solution Thermodynamics by Microcalorimetry

Cited by 2 publications

References 30 publications

Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-binding Domains of the ETS Family Transcription Factors Ets-1 and PU.1

Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-binding Domains of the ETS Family Transcription Factors Ets-1 and PU.1

ITC and SPR Analysis Using Dynamic Approach

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