An Exploration of Histone Molecular Evolution From The Static Accessibility of Amino Acid Residues
- Received Date: 1900-01-01
- Rev Recd Date: 1900-01-01
- Publish Date: 1997-11-22
Abstract: This paper investigated and discussed the evolutionary relations of four histone molecules,H[2A],H[2B],H and H with the static accessibilities of protein amino acid residues as an index.The phylogenetic trees of H[2A],H[2B] and H have been obtained.The results indicated that protein three-dimensional structure is more reliable as studing protein molecular evolution;in addition,H is the most conservative protein in the four histone molecules composing nucleosome.The authors speculate upon that histone H,as compared with other histones,perhaps has the most important significance both in keeping chromosomal structure and function and in the origin of chromosome.
|Citation:||HUANG Jing-fei, LIU Ci-quan. An Exploration of Histone Molecular Evolution From The Static Accessibility of Amino Acid Residues. Zoological Research, 1997, 18(4): 429-435.|