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Robust and convenient analysis of protein thermal and chemical stability
Author(s) -
Niklasson Markus,
Andresen Cecilia,
Helander Sara,
Roth Marie G.L.,
Zimdahl Kahlin Anna,
Lindqvist Appell Malin,
Mårtensson LarsGöran,
Lundström Patrik
Publication year - 2015
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2809
Subject(s) - denaturation (fissile materials) , biological system , stability (learning theory) , software , computer science , circular dichroism , graphical user interface , interface (matter) , chemical stability , documentation , chemistry , thermal stability , crystallography , programming language , gibbs isotherm , organic chemistry , adsorption , machine learning , nuclear chemistry , biology
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.