Quantum and experimental conformational analysis of model molecules related to collagenic structures |
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| Affiliation: | 1. ICSM, CNRS, CEA, Univ Montpellier, ENSCM, Marcoule, France;2. Division of Theoretical Chemistry, Lund University, POB 124, SE-221 00 Lund, Sweden;3. X-ray and Neutron Science, Niels Bohr Institute, University of Copenhagen, Denmark;4. Novozymes A/S, Denmark;5. LINXS – Lund Institute of Advanced Neutron and X-ray Science, Scheelevägen 19, SE-223 70 Lund, Sweden;1. Laboratoire Matrice Extracellulaire et Dynamique Cellulaire (MEDyC), UMR 7369, Université de Reims, Faculté des Sciences, Moulin de la Housse, 51687, Reims Cedex 2, France;2. Université Sorbonne Paris Nord, UFR Santé-Médecine-Biologie Humaine, Groupe de Biophysique Moléculaire, 74 Rue Marcel Cachin, 93017, Bobigny cedex, France;3. Laboratoire Jean-Perrin, Sorbonne Université, CNRS UMR 8237, 4 Place Jussieu, 75005, Paris, France |
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| Abstract: | Sequential polytripeptides comprising the repeating sequences (Gly-Pro-X) and (Gly-X-Pro) have been synthesized, and conformational analysis has been carried out using both quantum and experimental methods (X = Pro, Ala, Val, Ile R and Ile S, Leu, Nle, Met and Phe).PCILO computations were performed using appropriate model molecules, with a view to discussing the proline puckering, the cis/trans isomerism of Pro residue and the accessibility to different conformons (δ, Rα, Lα, β sheets and β bends) for the X residues, with the pyrrolidine rings free to adopt the most favorable puckering.Experimental studies show that, whatever sequence is considered in the triplet, the only ordered structures found are the obvious δ collagenlike structure and the β bend.Theoretical studies led to the conclusion that when Pro is in the δ conformation, the β bend is very probably of type II.On this basis, the microheterogeneity in collagen structure and the involvement of β bends in the enzymatic proline hydroxylation are discussed. |
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