ニュース

2015年12月04日 掲載 (Published 12/04/2015)


「Biophysics and Physicobiology」に Saki Aoto et al. “Case study on the evolution of hetero-oligomer interfaces based on the differences in paralogous proteins”を掲載

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Saki Aoto and Kei Yura
“Case study on the evolution of hetero-oligomer interfaces based on the differences in paralogous proteins”

【Significance】
Evolutionary Difference between Hetero- and Homo-oligomer interfaces

Proteins function in assembly in a cell, and the structural elucidation of the assemblies is the first step for the understanding of the biological mechanism of them. The mechanism of assembly formation has been computationally studied in the context of protein-protein interactions, especially in homo-oligomers. We focused on hetero-oligomers in this study and examined the differences in the oligomer interfaces in homo- and hetero-oligomers. In this case study, relatively weak trends, residue conservation and hydrophobicity, known in homo-oligomers in the previous studies are found to outstand in hetero-oligomers.


Biophysics and Physicobiology, Vol.12, pp. 103-116

URL:http://doi.org/10.2142/biophysico.12.0_103