Abstract
Although thermodynamic formalisms for protein denaturation have been established for some time, available software programs for deconvolution of DSC data exhibit various limitations. These include enforcing a constant deltaCp(T), linear heat capacity functions, and so on. We have developed a Windows based program that allows greater flexibility, speed and accuracy than previously available programs for the analysis of DSC data. One novel feature of the program is the inclusion of, and ability to refine, a concentration-dependent term.
Keywords: PROTEIN DENATURATION, differential scanning calorimetry (DSC), DSCFit
Protein & Peptide Letters
Title: An Efficient, Flexible-Model Program For The Analysis Of Differential Scanning Calorimetry Protein Denaturation Data
Volume: 8 Issue: 6
Author(s): Sasha B. Grek, John K. Davis and Michael Blaber
Affiliation:
Keywords: PROTEIN DENATURATION, differential scanning calorimetry (DSC), DSCFit
Abstract: Although thermodynamic formalisms for protein denaturation have been established for some time, available software programs for deconvolution of DSC data exhibit various limitations. These include enforcing a constant deltaCp(T), linear heat capacity functions, and so on. We have developed a Windows based program that allows greater flexibility, speed and accuracy than previously available programs for the analysis of DSC data. One novel feature of the program is the inclusion of, and ability to refine, a concentration-dependent term.
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Cite this article as:
Grek B. Sasha, Davis K. John and Blaber Michael, An Efficient, Flexible-Model Program For The Analysis Of Differential Scanning Calorimetry Protein Denaturation Data, Protein & Peptide Letters 2001; 8 (6) . https://dx.doi.org/10.2174/0929866013409184
DOI https://dx.doi.org/10.2174/0929866013409184 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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