ISBN: 9786207759118 - molecular modeling: deciphering the structural stability of human collagen (16 resultados)

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Taschenbuch. Condición: Neu. Molecular Modeling | Deciphering the Structural Stability of Human Collagen | Jonas Oliveira (u. a.) | Taschenbuch | Englisch | 2024 | Our Knowledge Publishing | EAN 9786207759118 | Verantwortliche Person für die EU: SIA OmniScriptum Publishing, Brivibas Gatve 197, 1039 RIGA, LETTLAND, customerservice[at]vdm-vsg[dot]de | Anbieter: preigu.…

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Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware 84 pp. Englisch.

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Taschenbuch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - In this work, the stability of the homotrimeric peptide T3-785, a representative model of human collagen, was described in energetic terms using the molecular fractionation with conjugated caps (MFCC) technique and within the scope of density functional theory (DFT). It was possible to predict the individual relevance of the amino acids Pro, Hyp, Gly, Ile, Thr, Gly, Ala, Arg, Gly, Leu and Ala, the consequent importance of the triads Pro-Hyp-Gly, Ile-Thr-Gly, Ala-Arg-Gly and Leu-Ala-Gly, and finally the influence of the N-terminal, Central and C-terminal zones of each chain in maintaining the integrity of the collagen triple helix. To make this possible, the forces of attraction and repulsion of the 90 residues that make up the system were calculated. Each of these residues had an interaction energy that varied depending on the chemical nature of its side chain, the microsolvation environment surrounding it and the intermolecular contacts it established. The pioneering study of the conformational stability in energetic terms of a free region of imino acids will encourage research focused on the development and synthesis of high-stability artificial collagens by Bioengineering. …

Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -In this work, the stability of the homotrimeric peptide T3-785, a representative model of human collagen, was described in energetic terms using the molecular fractionation with conjugated caps (MFCC) technique and within the scope of density functional theory (DFT). It was possible to predict the individual relevance of the amino acids Pro, Hyp, Gly, Ile, Thr, Gly, Ala, Arg, Gly, Leu and Ala, the consequent importance of the triads Pro-Hyp-Gly, Ile-Thr-Gly, Ala-Arg-Gly and Leu-Ala-Gly, and finally the influence of the N-terminal, Central and C-terminal zones of each chain in maintaining the integrity of the collagen triple helix. To make this possible, the forces of attraction and repulsion of the 90 residues that make up the system were calculated. Each of these residues had an interaction energy that varied depending on the chemical nature of its side chain, the microsolvation environment surrounding it and the intermolecular contacts it established. The pioneering study of the conformational stability in energetic terms of a free region of imino acids will encourage research focused on the development and synthesis of high-stability artificial collagens by Bioengineering.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 84 pp. Englisch. …