Robust and convenient analysis of protein thermal and chemical stability
2015 (English)In: Protein Science, ISSN 0961-8368, E-ISSN 1469-896X, Vol. 24, no 12, 2055-2062 p.Article in journal (Refereed) PublishedText
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.
Place, publisher, year, edition, pages
WILEY-BLACKWELL , 2015. Vol. 24, no 12, 2055-2062 p.
protein stability; thermal denaturation; chemical denaturation; circular dichroism; fluorescence; curve fitting; protein stability software; protein denaturation software
Chemical Sciences Clinical Medicine
IdentifiersURN: urn:nbn:se:liu:diva-124648DOI: 10.1002/pro.2809ISI: 000368292000014PubMedID: 26402034OAI: oai:DiVA.org:liu-124648DiVA: diva2:901583
Funding Agencies|Swedish Research Council [2012-5136]; LiU Cancer2016-02-082016-02-082016-03-01