Electric dipole moments and conformations of isolated peptides
| Autor: | Driss Rayane, Rodolphe Antoine, Ph. Dugourd, Frederick C. Hagemeister, Martin F. Jarrold, Michel Broyer, Gary A. Breaux, David Pippen, Isabelle Compagnon, Robert R. Hudgins |
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| Přispěvatelé: | Laboratoire de Spectrométrie Ionique et Moléculaire (LASIM), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
Materials science 010304 chemical physics Tryptophan Peptide Plasma 010402 general chemistry 01 natural sciences Atomic and Molecular Physics and Optics 0104 chemical sciences Crystallography Dipole chemistry Polarizability Ab initio quantum chemistry methods Electric field 0103 physical sciences PACS. 87.15.-v Biomolecules: structure and physical properties - 33.15.Kr Electric and magnetic moments (and derivatives) polarizability and magnetic susceptibility Molecular beam |
| Zdroj: | The European Physical Journal D : Atomic, molecular, optical and plasma physics The European Physical Journal D : Atomic, molecular, optical and plasma physics, EDP Sciences, 2002, 20 (3), pp.583-587. ⟨10.1140/epjd/e2002-00149-4⟩ |
| ISSN: | 1434-6079 1434-6060 |
| Popis: | International audience; The electric dipole moments of the isolated amino acid tryptophan and small glycine-based peptides (WGn, n = 1-5, W = tryptophan, G = glycine) have been measured by deflection of a molecular beam in an inhomogeneous electric field. The measurements are compared to the results of ab initio calculations and Monte-Carlo simulations. The conformation and the flexibility of the peptides, at different temperatures, are discussed. The WGn peptides are much more floppy than an isolated tryptophan, even a single glycine is enough to make the peptide floppy on the timescale of the electric deflection measurements. |
| Databáze: | OpenAIRE |
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