Robust and convenient analysis of protein thermal and chemical stability

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...

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Bibliographic Details
Published in:Protein science 2015-12, Vol.24 (12), p.2055-2062
Main Authors: Niklasson, Markus, Andresen, Cecilia, Helander, Sara, Roth, Marie G.L., Zimdahl Kahlin, Anna, Lindqvist Appell, Malin, Mårtensson, Lars‐Göran, Lundström, Patrik
Format: Article
Language:English
Subjects:
chemical denaturation
Circular Dichroism
Computational Biology - methods
curve fitting
Denaturation
Dichroism
fluorescence
Fluorescence spectroscopy
Graphical user interface
Methods and Applications
Models, Molecular
Protein Denaturation
protein denaturation software
Protein Stability
protein stability software
Proteins
Proteins - chemistry
Software
Spectrometry, Fluorescence
Stability analysis
Temperature
thermal denaturation
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Summary: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.
ISSN:0961-8368
1469-896X
1469-896X
DOI:10.1002/pro.2809