Helix‐coil stability constants for the naturally occurring amino acids in water. XII. Asparagine parameters from random poly(hydroxybutylglutamine‐co‐ L ‐asparagine) | Zendy

Matheson R. R. | Zendy; Nemenoff R. A. | Zendy; Cardinaux F. | Zendy; Scheraga H. A. | Zendy

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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.

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