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Using a second‐order differential model to fit data without baselines in protein isothermal chemical denaturation

protein stability studies are commonly conducted via thermal or chemical denaturation/renaturation of protein. Conventional data analyses on the protein unfolding/(re)folding require well‐defined pre‐ and post‐transition baselines to evaluate Gibbs free‐energy change associated with the protein unfo... Full description

Journal Title: Protein Science April 2016, Vol.25(4), pp.898-904
Main Author: Tang, Chuanning
Other Authors: Lew, Scott , He, Dacheng
Format: Electronic Article Electronic Article
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ID: ISSN: 0961-8368 ; E-ISSN: 1469-896X ; DOI: 10.1002/pro.2878
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recordid: wj10.1002/pro.2878
title: Using a second‐order differential model to fit data without baselines in protein isothermal chemical denaturation
format: Article
creator:
  • Tang, Chuanning
  • Lew, Scott
  • He, Dacheng
subjects:
  • Protein Unfolding
  • Chemical Denaturation
  • Baselines‐Missing
  • Second‐Order Derivative Data Analysis
ispartof: Protein Science, April 2016, Vol.25(4), pp.898-904
description: protein stability studies are commonly conducted via thermal or chemical denaturation/renaturation of protein. Conventional data analyses on the protein unfolding/(re)folding require well‐defined pre‐ and post‐transition baselines to evaluate Gibbs free‐energy change associated with the protein unfolding/(re)folding. This evaluation becomes problematic when there is insufficient data for determining the pre‐ or post‐transition baselines. In this study, fitting on such partial data obtained in protein chemical denaturation is established by introducing second‐order differential (SOD) analysis to overcome the limitations that the conventional fitting method has. By reducing numbers of the baseline‐related fitting parameters, the SOD analysis can successfully fit incomplete chemical denaturation data sets with high agreement to the conventional evaluation on the equivalent completed data, where the conventional fitting fails in analyzing them. This SOD fitting for the abbreviated isothermal chemical denaturation further fulfills data analysis methods on the insufficient data sets conducted in the two prevalent protein stability studies.
language:
source:
identifier: ISSN: 0961-8368 ; E-ISSN: 1469-896X ; DOI: 10.1002/pro.2878
fulltext: fulltext
issn:
  • 0961-8368
  • 09618368
  • 1469-896X
  • 1469896X
url: Link


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titleUsing a second‐order differential model to fit data without baselines in protein isothermal chemical denaturation
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subjectProtein Unfolding ; Chemical Denaturation ; Baselines‐Missing ; Second‐Order Derivative Data Analysis
descriptionprotein stability studies are commonly conducted via thermal or chemical denaturation/renaturation of protein. Conventional data analyses on the protein unfolding/(re)folding require well‐defined pre‐ and post‐transition baselines to evaluate Gibbs free‐energy change associated with the protein unfolding/(re)folding. This evaluation becomes problematic when there is insufficient data for determining the pre‐ or post‐transition baselines. In this study, fitting on such partial data obtained in protein chemical denaturation is established by introducing second‐order differential (SOD) analysis to overcome the limitations that the conventional fitting method has. By reducing numbers of the baseline‐related fitting parameters, the SOD analysis can successfully fit incomplete chemical denaturation data sets with high agreement to the conventional evaluation on the equivalent completed data, where the conventional fitting fails in analyzing them. This SOD fitting for the abbreviated isothermal chemical denaturation further fulfills data analysis methods on the insufficient data sets conducted in the two prevalent protein stability studies.
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titleUsing a second‐order differential model to fit data without baselines in protein isothermal chemical denaturation
descriptionprotein stability studies are commonly conducted via thermal or chemical denaturation/renaturation of protein. Conventional data analyses on the protein unfolding/(re)folding require well‐defined pre‐ and post‐transition baselines to evaluate Gibbs free‐energy change associated with the protein unfolding/(re)folding. This evaluation becomes problematic when there is insufficient data for determining the pre‐ or post‐transition baselines. In this study, fitting on such partial data obtained in protein chemical denaturation is established by introducing second‐order differential (SOD) analysis to overcome the limitations that the conventional fitting method has. By reducing numbers of the baseline‐related fitting parameters, the SOD analysis can successfully fit incomplete chemical denaturation data sets with high agreement to the conventional evaluation on the equivalent completed data, where the conventional fitting fails in analyzing them. This SOD fitting for the abbreviated isothermal chemical denaturation further fulfills data analysis methods on the insufficient data sets conducted in the two prevalent protein stability studies.
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titleUsing a second‐order differential model to fit data without baselines in protein isothermal chemical denaturation
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abstractprotein stability studies are commonly conducted via thermal or chemical denaturation/renaturation of protein. Conventional data analyses on the protein unfolding/(re)folding require well‐defined pre‐ and post‐transition baselines to evaluate Gibbs free‐energy change associated with the protein unfolding/(re)folding. This evaluation becomes problematic when there is insufficient data for determining the pre‐ or post‐transition baselines. In this study, fitting on such partial data obtained in protein chemical denaturation is established by introducing second‐order differential (SOD) analysis to overcome the limitations that the conventional fitting method has. By reducing numbers of the baseline‐related fitting parameters, the SOD analysis can successfully fit incomplete chemical denaturation data sets with high agreement to the conventional evaluation on the equivalent completed data, where the conventional fitting fails in analyzing them. This SOD fitting for the abbreviated isothermal chemical denaturation further fulfills data analysis methods on the insufficient data sets conducted in the two prevalent protein stability studies.
doi10.1002/pro.2878
pages898-904
date2016-04