The incorporation of alpha-amino acids with a quaternary alpha-carbon atom into a peptide provides a tool to effectively restrict the available range of its backbone conformations. Specifically, under favorable conditions, Calpha,alpha-diethylglycine (Deg) homopeptides are known to preferentially adopt the fully-extended (2.05-helical) structure, which is characterized by the longest possible separation between two adjacent alpha-amino acid Cα atoms. We have investigated the influence of the nature of the N- and/or C-terminal protecting (or blocking) groups on the relative stabilities of the fully-extended conformation vs. the competing, shorter 3(10)-helical structure in a synthetic Deg homopeptide series.
Looking for a Robust, Synthetic, Fully-Extended (2.05-Helical) Peptide Structure - Effect of Terminal Groups
FORMAGGIO, FERNANDO;PEGGION, CRISTINA;MORETTO, ALESSANDRO;TONIOLO, CLAUDIO
2012
Abstract
The incorporation of alpha-amino acids with a quaternary alpha-carbon atom into a peptide provides a tool to effectively restrict the available range of its backbone conformations. Specifically, under favorable conditions, Calpha,alpha-diethylglycine (Deg) homopeptides are known to preferentially adopt the fully-extended (2.05-helical) structure, which is characterized by the longest possible separation between two adjacent alpha-amino acid Cα atoms. We have investigated the influence of the nature of the N- and/or C-terminal protecting (or blocking) groups on the relative stabilities of the fully-extended conformation vs. the competing, shorter 3(10)-helical structure in a synthetic Deg homopeptide series.
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