Helix-coil stability constants for the naturally occurring amino acids in water. 11. Lysine parameters from random poly(hydroxybutylglutamine-co-L-lysine).
The synthesis and characterization of water-soluble random copolymers containing L-lysine with N5-(4-hydroxybutyl)-L-glutamine, and the thermally induced helix-coil transitions of these copolymers in water, are described. The incorporation of L-lysine was found to decrease the helix content of the polymers at neutral pH. The Zimm-Bragg parameters sigma and s for the helix-coil transition in poly(L-lysine) in water were deduced from an analysis of the melting curves in the manner described in earlier papers. The computed values of s indicate that, in the temperature range of 0-60 degrees C, lysine has a tendency to destabilize helical sequences, this tendency being minimal at approximately 25 degrees C and increasing at lower and higher temperatures.
D002151:Calorimetry; D002942:Circular Dichroism; D005973:Glutamine / Q000031:analogs & derivatives; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine; D008970:Molecular Weight; D009905:Optical Rotatory Dispersion; D010455:Peptides; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics
D010455:Peptides; D005973:Glutamine; D008239:Lysine