Bioinformatic Analysis of Structure and Function of MEPE
HUANG Yan1, LI Yu-Na1, REN Chen-Xia1, WANG Jun-Mei1, HUANG Xuan-Yi1, SONG Li-Hua2
1. School of Preclinical Medicine, Changzhi Medical College, Changzhi 046000, China;
2. Department of Pharmacology, Changzhi Medical College, Changzhi 046000, China
Abstract The structure and function of MEPE protein were analyzed by bioinformatics methods, including physical and chemical properties, the subcellular position, transmembrane region, signal peptide, spatial structure, protein interaction networks and evolutionary tree. The analysis showed that the isoelectric point of human MEPE protein was 8.62, which was an alkaline hydrophilic protein theoretically, with signal peptide area and no transmembrane region, belonged to secretory protein. The main secondary structure element was random coil. MEPE was highly conservative in mammals and could interact with many proteins.
HUANG Yan, LI Yu-Na, REN Chen-Xia, WANG Jun-Mei, HUANG Xuan-Yi, SONG Li-Hua. Bioinformatic Analysis of Structure and Function of MEPE[J]. Chinese Journal of Chemical Education, 2019, 40(10): 82-86.
