Structures of Cu(I1) complexes of pyridoxal Schiff bases with poly(L-lysine), poly(L-ornithine), and poly(L-a,?-diaminobutyric acid) were investigated by absorption spectra, CD, and conformational analysis. Although the polypeptides retain their typical right-handed a-helical conformation, opposite
Conformational studies on the pyridoxal Schiff bases of polypeptides
✍ Scribed by M. Dentini; G. Perretti; M. Savino; P. De Santis; A. S. Verdini
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1978
- Tongue
- English
- Weight
- 520 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
The pyridoxal Schiff bases of the polypeptides poly(L-lysine), poly(L-ornithine), and poly(L-a,y-diaminobutyric acid) were prepared and investigated in water/methanol by CD spectra and equilibrium dialysis experiments. Only the poly(L-a,?-diaminobutyric acid) derivative is characterized by a relevant optical activity similar to that found in pyridoxal enzymes. The stereospecific interactions between the pyridoxylideneimine group and the polypeptide chain prevent the hydrolysis reaction of the aldimine bond.
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