Publication: Computational analysis of homo-dimerization of chloroplast-localized chaperonin from the alga Chlamydomonas reinhardtii
Issued Date
2021-01-01
Resource Type
ISSN
2452316X
24681458
24681458
Other identifier(s)
2-s2.0-85121758897
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Agriculture and Natural Resources. Vol.55, No.5 (2021), 724-733
Suggested Citation
Rungdawan Wongsamart, Duangnapa Kiriwan, Chonticha Suwattanasophon, Kittisak Yokthongwattana, Kiattawee Choowongkomon Computational analysis of homo-dimerization of chloroplast-localized chaperonin from the alga Chlamydomonas reinhardtii. Agriculture and Natural Resources. Vol.55, No.5 (2021), 724-733. doi:10.34044/j.anres.2021.55.5.03 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/75756
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Computational analysis of homo-dimerization of chloroplast-localized chaperonin from the alga Chlamydomonas reinhardtii
Other Contributor(s)
Abstract
Molecular chaperones are major groups of proteins responsible for proteostasis regulation. GroEL is a protein belonging to the chaperonin family of molecular chaperones. Unlike GroEL in prokaryotes, chloroplast chaperonin 60 (Cpn60) has distinct subunits. The chaperonin for the alga Chlamydomonas reinhardtii has one α and two β subunits (β1 and β2). Even though a crystal structure of homo-oligomer (Cpn60β1) has been reported, it is still unclear how these subunits assemble. This study modeled homo-subunit dimers of C. reinhardtii. Dimers αα, β1β1 and β2β2 were analyzed based on molecular dynamics simulation. Many hydrogen bonds presented in the same position among the three dimers, even though the amino acids were different. Charged amino acids were an important factor influencing the binding interface orientation. The binding free energy of the β1β1 dimer was the lowest, followed by β2β2 and αα, respectively. The results suggested that the β1β1 assembly was more favorable than β2β2 and αα.