Premium
Helix‐coil stability constants for the naturally occurring amino acids in water. XII. Asparagine parameters from random poly(hydroxybutylglutamine‐co‐ L ‐asparagine)
Author(s) -
Matheson R. R.,
Nemenoff R. A.,
Cardinaux F.,
Scheraga H. A.
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360160715
Subject(s) - chemistry , asparagine , random coil , helix (gastropod) , amino acid , stability (learning theory) , stereochemistry , crystallography , circular dichroism , biochemistry , ecology , snail , machine learning , computer science , biology
The synthesis and characterization of water‐soluble random copolymers containing L ‐asparagine with N 5 ‐(4‐hydroxybutyl)‐ L ‐glutamine, and the thermally induced helix‐coil transitions of these copolymers in water, are described. The incorporation of L ‐asparagine was found to decrease the helix content of the polymers in water at all temperatures. The Zimm‐Bragg parameters σ and s for the helix‐coil transition in poly( L ‐asparagine) in water were deduced from an analysis of the copolymer melting curves in the manner described in earlier papers. The computed values of s indicate that asparagine destabilizes helical sequences at all temperatures in the range 0–60°C.