| Autor: |
Rsu Wasagu, M Lawal, CH Njoku, M.K Abubakar |
| Rok vydání: |
2011 |
| Předmět: |
|
| Zdroj: |
Nigerian Journal of Basic and Applied Sciences; Vol 18, No 2 (2010) |
| ISSN: |
0794-5698 |
| Popis: |
The spectra of amide I region (1700-1600cm-1) of horse heart ferricytochrome c at 20oC are reported at low ionic strength at of pH values between 7.0 and 11.5 encompassing the alkaline transition. The mid-infrared spectra can probe the protein secondary structures. The Fourier transform infrared spectroscopic technique is used to investigate the changes in the conformationally sensitive amide I band of cytochrome c with pH and ionic strength. Analysis of these results supports the hypothesis that an increase in the non-repetitive secondary structure during alkaline transition is at the expense of regular secondary structures. These strongly suggest that structural switching and ligand exchange behaviour of ferricytochrome c is accompanied by conformational change in the protein backbone |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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