Reassessment of the electronic circular dichroism criteria for random coil conformations of poly(L-lysine) and the implications for protein folding and denaturation studies.
The circular dichroism (CD) spectra of poly(L-lysine) in water and ethanediol/water (2:1) solutions in the temperature range -110 to 85 degrees C are presented. The results combined with vibrational CD data are interpreted in terms of a two-state conformational equilibrium with a left-handed trans polyproline II conformation being preferred at low temperatures. The relevance of these studies to the CD criteria for random-coil conformations, the study of helix-coil transitions and protein/peptide folding is pointed out.
Drake
A F
AF
Department of Chemistry, Birkbeck College, London, U.K.
Siligardi
G
G
Gibbons
W A
WA
D002942:Circular Dichroism; D011107:Polylysine; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
D011107:Polylysine