On the flexibility of beta-peptides |
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Authors: | Beke Tamás Csizmadia Imre G Perczel András |
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Institution: | 1. Department of Organic Chemistry, Eötvös L. Univ. P.O. Box 32, H-1518 Budapest 112, Hungary;2. Department of Organic Chemistry, Eötvös L. Univ. P.O. Box 32, H-1518 Budapest 112, Hungary
Department of Chemistry, University of Toronto, Ontario, M5S 1A1, Canada |
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Abstract: | The full conformational space was explored for an achiral and two chiral beta-peptide models: namely For-beta-Ala-NH2, For-beta-Abu-NH2, and For-beta-Aib-NH2. Stability and conformational properties of all three model systems were computed at different levels of theory: RHF/3-21G, B3LYP/6-311++G(d,p)//RHF/3-21G, B3LYP/6-311++G(d,p), MP2//B3LYP/6-311++G(d,p), CCSD//B3LYP/6-311++G(d,p), and CCSD(T)//B3LYP/6-311++G(d,p). In addition, ab initio E = E(phi, micro, psi) potential energy hypersurfaces of all three models were determined, and their topologies were analyzed to determine the inherent flexibility properties of these beta-peptide models. Fewer points were found and assigned than expected on the basis of Multidimensional Conformational Analysis (MDCA). Furthermore, it has been demonstrated, that the four-dimensional surface, E = E(phi, mu, psi), can be reduced into a three-dimensional one: E = Ephi, f(phi), psi]. This reduction of dimensionality of freedom of motion suggests that beta-peptides are less flexible than one would have thought. This agrees with experimental data published on the conformational properties of peptides composed of beta-amino acid residues. |
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Keywords: | β-peptides ab initio and DFT computation structure and stability Ramachandran surface flexibility conformation and topology β-amino acids |
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