Intrinsic Folding of Small Peptide Chains: Spectroscopic Evidence for the Formation of Beta-turns in the Gas PhaseReport as inadecuate




Intrinsic Folding of Small Peptide Chains: Spectroscopic Evidence for the Formation of Beta-turns in the Gas Phase - Download this document for free, or read online. Document in PDF available to download.

1 LFP - URA 2453 - Laboratoire Francis PERRIN

Abstract : Laser desorption of model peptides coupled to laser spectroscopic techniques enables the gas-phase observation of genuine secondary structures of biology. Spectroscopic evidence for the formation of -turns in gas-phase peptide chains containing glycine and phenylalanine residues establishes the intrinsic stability of these forms and their ability to compete with other stable structures. The precise characterization of local minima on the potential energy surface from IR spectroscopy constitutes an acute assessment for the state-of-the-art quantum mechanical calculations also presented. The observation of different types of -turns depending upon the residue order within the sequence is found to be consistent with the residue propensities in -turns of proteins, which suggests that the prevalence of glycine in type II and II- turns stems essentially from an energetic origin, already at play under isolated conditions.

Keywords : Protected peptide beta-turn UV spectroscopy IR spectroscopy





Author: W. Chin, - Jean-Pierre Dognon - Fran├žois Piuzzi - Benjamin Tardivel - Iliana Dimicoli - Michel Mons -

Source: https://hal.archives-ouvertes.fr/



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