Biophysical analysis of the effect of chemical modification by 4-oxononenal on the structure, stability, and function of binding immunoglobulin protein (BiP)
Fig 4
(A) Changes in the CD signal at 222 nm as a function of urea concentration. (B) Changes in the CD signal at 222 nm as a function of solution temperature. (C) Changes in the protein fluorescence at 364 nm as a function of urea concentration. (D) Changes in the protein fluorescence at 330 nm as a function of solution temperature. (E) Changes in the specific heat capacity of the protein as a function of increasing temperature as measured by DSC. The deconvolution fits are indicated as dashed lines. In all panels, black and red colors indicate the data for wild-type BiP and chemically modified BiP, respectively.