MOLECULAR DYNAMICS RESEARCH ON R175 RESIDUE SUBSTITUTION IN P53 PROTEIN
P53蛋白质R175残基替换的分子动力学研究

The molecular dynamics research of the core domain of p53 protein crystal structure shows that besides the stability in biochemistry this domain also shows a high stability in molecular mechanics. Based on this work, we substituted the residue R175 with some other amino acids and performed molecular dynamics researches separately. The results show that substitution of R175 causes a relax tendency between loop2 and 3 domains, leading to an alteration of the whole conformation of p53 core domain and ruining its stability. This research visually explains the mechanism of p53 changes in immunological and biochemical reactions, which are caused by R175 substitutions leading to the 3-D structure variations.