Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. 20. Reinvestigation of Valine Parameters From Random Poly((Hydroxypropyl)Glutamine-co-L-Valine)

Even though L-valine and L-isoleucine are both beta -branched amino acids, the effect of temperature on their helix-forming tendency differs markedly. Since this apparent anomaly might have arisen from significant nonrandom incorporation of L-valine into the copolymer used previously to determine it...

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Bibliographic Details
Published inMacromolecules Vol. 14; no. 3; pp. 633 - 634
Main Authors Chang, M C, Fredrickson, R A, Powers, S P, Scheraga, HA
Format Journal Article
LanguageEnglish
Published 01.01.1981
Subjects
helix-coil transitions
poly((hydroxypropyl)glutamine-co-L-valine)
synthesis
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Summary:Even though L-valine and L-isoleucine are both beta -branched amino acids, the effect of temperature on their helix-forming tendency differs markedly. Since this apparent anomaly might have arisen from significant nonrandom incorporation of L-valine into the copolymer used previously to determine its helix-coil stability constants, this copolymer is reinvestigated here, using a different method of synthesis to avoid formation of large, nonrandom blocks of L-valine. Within experimental error, the same temperature dependence of the Zimm-Bragg parameter s for L-valine is obtained as found with the copolymer synthesized in earlier work. The difference in the behavior between L-valine and L-isoleucine is therefore a real one.
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ISSN:0024-9297