| Literature DB >> 26402034 |
Markus Niklasson1, Cecilia Andresen1, Sara Helander2, Marie G L Roth1, Anna Zimdahl Kahlin2, Malin Lindqvist Appell2, Lars-Göran Mårtensson1, Patrik Lundström1.
Abstract
We present the software CDpal that is used to analyze thermal and chemical denaturation data to obtain information on protein stability. The software uses standard assumptions and equations applied to two-state and various types of three-state denaturation models in order to determine thermodynamic parameters. It can analyze denaturation monitored by both circular dichroism and fluorescence spectroscopy and is extremely flexible in terms of input format. Furthermore, it is intuitive and easy to use because of the graphical user interface and extensive documentation. As illustrated by the examples herein, CDpal should be a valuable tool for analysis of protein stability.Keywords: chemical denaturation; circular dichroism; curve fitting; fluorescence; protein denaturation software; protein stability; protein stability software; thermal denaturation
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Year: 2015 PMID: 26402034 PMCID: PMC4815239 DOI: 10.1002/pro.2809
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725