Abstract
The FTIR spectral measurements were carried out for native cytochrome c (cyt c) and its four platinum-modified derivatives. The influence of the platinum complex binding on the secondary structure of cyt c was discussed. It was found that the secondary structure of platinum-binded derivatives is similar to that of native cyt c when the platinum complex is binding on or near the surface of the protein. While in the case of derivatives, in which the platinum complex interacts with the second axial ligand of cyt c (Met 80) and causes the replacement of Met 80 by Lys 79 or solvent (H2O), great secondary structural changes were observed. The results imply that the Met 80 residue is very important in controlling the secondary structure of cyt c.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
