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pubmed-article:7664050pubmed:abstractTextArginine is a stabilizing element in both thermophilic and low molecular weight proteins. Similarly Lys+-->Arg+ substitutions increase the helix content of designed helical peptides. Here we explore this 'arginine effect' by examining how Lys+-->Arg+ substitutions influence the 3(10)-helix-->alpha-helix equilibrium in the helical peptide Ac-(AAAAK)3A-NH2. The unsubstituted sequence contains a significant amount of 3(10)-helix, however, single Lys+-->Arg+ substitutions shift the peptide conformation toward alpha-helix in a position-dependent fashion. The single substitution closest to the carboxy terminus induces the largest conformational change at the helix amino terminus. These findings suggest that a single strategically-placed arginine can exert long range control on helix structure.lld:pubmed
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pubmed-article:7664050pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:7664050pubmed:articleTitleA single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide.lld:pubmed
pubmed-article:7664050pubmed:affiliationDepartment of Chemistry and Biochemistry, University of California, Santa Cruz 95064, USA.lld:pubmed
pubmed-article:7664050pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7664050pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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