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. Author manuscript; available in PMC: 2009 Aug 20.

Published in final edited form as: Biochemistry. 2008 Apr 8;47(17):4887–4897. doi: 10.1021/bi702211j

Analysis of the stability of the kinase domain. Samples were prepared at 0.15 mg/ml and variable urea concentrations and incubated at 20°C for 3 hours. Unfolding was monitored using CD at 222 nm () and tryptophan fluorescence emission with excitation at 295 and emission at 340 nm (). A) Raw data. B) Background subtracted and normalized data. The lines are the global fit of the CD and fluorescence data to a three-state model obtained using SAVUKA.

Inline graphic — Analysis of the stability of the kinase domain. Samples were prepared at 0.15 mg/ml and variable urea concentrations and incubated at 20°C for 3 hours. Unfolding was monitored using CD at 222 nm () and tryptophan fluorescence emission with excitation at 295 and emission at 340 nm (). A) Raw data. B) Background subtracted and normalized data. The lines are the global fit of the CD and fluorescence data to a three-state model obtained using SAVUKA.