Natural Leather Protein's Thermal Stability at High Temperature Conditions: Analyzed by AMBER Software

In this paper, the model of a molecule of 1 cgd 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 proteinfs performance under high temperature.