Heterocyclic peptide backbone modifications in an alpha-helical coiled coil.
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ABSTRACT:
SUBMITTER: Horne WS
PROVIDER: S-EPMC1868409 | biostudies-literature | 2004 Dec
REPOSITORIES: biostudies-literature
Publications
Heterocyclic peptide backbone modifications in an alpha-helical coiled coil.
Horne W Seth WS Yadav Maneesh K MK Stout C David CD Ghadiri M Reza MR
Journal of the American Chemical Society 20041201 47
In this paper, we present 1,2,3-triazole epsilon2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known alpha-helical coiled coil. Biophysical characterization indicates that the modified peptides retain much of the helical structure of the parent sequence, and that the thermodynamic stability of the coiled coil depends on the position of the incorporation of the epsilon-residue. Crystal structures obtained for each peptide give insight into the chemical ...[more]
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