Circular dichroism study of NaSCN effect on conformation of poly-L-lysine.
Effects of NaSCN, urea and KCl on alpha, beta and random conformations of poly-L-lysine (PLL) in water at room temperature were examined and compared quantitatively on the basis of the rotational strength of maximal peak by means of circular dichroism (CD) measurement. Alpha and beta helical conformational change of PLL was markedly concentration dependent in both the cases of NaSCN and urea, but not KCl. Among these salts, the distortion potency of millimolar concentrations of NaSCN on both alpha and beta conformations was undoubtedly several hundred times stronger than for the other salts, showing a slightly lesser effect on the alpha conformation as compared with that on the beta helical one, while there was no significant effect on random conformations even in maximal salt concentrations. The concentration required to alter the peptide conformation was substantially smaller for urea than for KCl, but both urea and KCl exhibited more effectiveness on alpha than beta conformation in contrast to NaSCN throughout the respective concentrations.
D002942:Circular Dichroism; D007700:Kinetics; D011107:Polylysine; D011487:Protein Conformation; D012492:Salts; D013861:Thiocyanates
D012492:Salts; D013861:Thiocyanates; D011107:Polylysine; C024553:sodium thiocyanate