Abstract:
The isoforms of Myosin heavy chain（MyHC）expressed in adult skeletal muscle fibers were analyzed by using of bioinformatics tools, and then the evolutionary tree was built according to the result of correlative sequence alignments, the purpose of the work is to analyze structure and function of the proteins. The results show that there are various forms of MyHC in skeletal muscle of adult mice, and few differences in the physicochemical characteristics. Relatively more glycosylation sites are found and the main glycosylation sites are N-glycosylation sites. Moreover, mouse MyHCs contain multiple conservative domains such as motor-domain superfamily, MYSc, Myosin tail 1, etc.. Three states exist in their secondary structures: helix, coil and strand, their tertiary structures are similar. The phylogenetic tree results show that MyHCⅡb and MyHCⅠmight be more original compared with other MyHCs because of its larger difference of sequences and farther branch length. The plasticity of muscles becomes possible as a result of various forms of MyHC and few differences in the structure.
