An Efficient, Flexible-Model Program For The Analysis Of Differential Scanning Calorimetry Protein Denaturation Data

Authors: Grek S.B.; Davis J.K.; Blaber M.

Source: Protein and Peptide Letters, Volume 8, Number 6, December 2001 , pp. 429-436(8)

Publisher: Bentham Science Publishers

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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

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409184

Publication date: 2001-12-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.