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Robust and convenient analysis of protein thermal and chemical stability.

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.

SUBMITTER: Niklasson M

PROVIDER: S-EPMC4815239 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

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Robust and convenient analysis of protein thermal and chemical stability.

Niklasson Markus M Andresen Cecilia C Helander Sara S Roth Marie G L MG Zimdahl Kahlin Anna A Lindqvist Appell Malin M Mårtensson Lars-Göran LG Lundström Patrik P

Protein science : a publication of the Protein Society 20151010 12

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 ...[more]

PMID: 26402034

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