کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5371850 | 1503969 | 2008 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Sequence and stability of the goat cytochrome c Sequence and stability of the goat cytochrome c](/preview/png/5371850.png)
We have determined the sequence of mitochondrial cytochrome c (cyt-c) from the goat heart, and it was found to have a unique amino acid sequence among all amino acid sequences of cyt-c reported till date. Its sequence alignment with the bovine cytochrome c (b-cyt-c) led us to conclude that the goat cytochrome c (g-cyt-c) differs in amino acid sequence from b-cyt-c at only one position, i.e., Pro44(bovine) â Ala44(goat). It has been observed that guanidinium chloride (GdmCl) induces a two-state transition between the native (N) and denatured (D) states of g-cyt-c. This conclusion is reached from the coincidence of GdmCl-induced transition curves monitored by measurements of absorbance at 405, 530 and 695Â nm and circular dichroism (CD) at 222, 416 and 405Â nm. Analysis of denaturation curves for the Gibbs energy of stabilization suggests that the stability of g-cyt-c is, within experimental errors, identical to that of b-cyt-c. We have also measured the effect of temperature on the equilibrium, N state â D state of g-cyt-c in the presence of different GdmCl concentrations. These measurements gave values of transition temperature (Tm), changes in enthalpy (ÎHm) and heat capacity (ÎCp) of g-cyt-c in the absence of GdmCl, which are compared with those of b-cyt-c. We have used crystal structure coordinates of b-cyt-c to predict the structure and stability of g-cyt-c, which are compared with those of the bovine protein.
Journal: Biophysical Chemistry - Volume 138, Issues 1â2, November 2008, Pages 23-28