| Titre : |
Natural leather protein's thermal stability at high temperature conditions : analyzed by AMBER software |
| Type de document : |
texte imprimé |
| Auteurs : |
Zhong Anhua, Auteur ; Wan Luo, Auteur ; Jiang Xuewei, Auteur ; Hu Yuqin, Auteur ; Jinjin Li, Auteur |
| Année de publication : |
2016 |
| Article en page(s) : |
p. 238-240 |
| Note générale : |
Bibliogr. |
| Langues : |
Anglais (eng) |
| Catégories : |
Collagène
Cuirs et peaux -- Analyse
Hautes températures
Stabilité thermique
|
| Index. décimale : |
675 Technologie du cuir et de la fourrure |
| Résumé : |
In this paper, the model of a molecule of 1cgd collagen at high temperature was built using AMBER software. The software condition was set with 99 Amber force field, free boundary and Canonical ensemble (NVT), the time step as 1 femtosecond. The simulation indicates that the spatial conformation changes with rising temperature. The stability of collagen decreases and the spatial configuration deviation from the native conformation increases when the temperature rises. The structure of collagen I tends to be looser as the temperature increases and the contacts between protein molecules fall. The simulation also shows that, the more contacts between molecules, the better stability of the structure and the lower molecule activity. The decline of intermolecular hydrogen causes the decline of collagen I stability. In this paper, the thermal stability of natural leather was analyzed from the microscopic view which is helpful for understanding the changes of leather proteinis performance under high temperature. |
| Note de contenu : |
- Trajectory analysis of 1cgd collagen under different temperatures
- The contact number (Cn) analysis |
| En ligne : |
https://drive.google.com/file/d/1r-1TAaKVj7OtHzq-yX2PaGftSX4kyQG4/view?usp=drive [...] |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=27087 |
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 100, N° 5 (09-10/2016) . - p. 238-240
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