Abstract
The Cu(II) interactions with four tetrapeptides: Ala-Ala-Ala-Ala, Ala-Ala-Ala-Pro, Ala-Ala-Pro-Ala, and Pro-Ala-Ala-Ala were studied by the absorption, circular dichroism, and electron paramagnetic resonance spectra. The results clearly show that proline residue is a specific structural factor in the formed complexes and, on the other hand, it is a break point in the metal ion coordination to the consecutive peptide bond nitrogens. The only position of proline residue ina peptide sequence that makes proline nitrogen available for the metal ion coordination is the N-terminal position. But even in this case (i.e., in the Cu(II) Pro-Ala-Ala-Ala system) proline plays a critical role in the creation of the specific structures in the complex formed in solution.
Sign-in/Register to access full text options 
Free) 
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 call
