文章基本信息

标题：Protein evolution analysis of S-hydroxynitrile lyase by complete sequence design utilizing the INTMSAlign software
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作者：Shogo Nakano ; Yasuhisa Asano
期刊名称：Scientific Reports
电子版ISSN：2045-2322
出版年度：2015
卷号：5
期号：1
DOI：10.1038/srep08193
语种：English
出版社：Springer Nature
摘要：Development of software and methods for design of complete sequences of functional proteins could contribute to studies of protein engineering and protein evolution. To this end, we developed the INTMSAlign software, and used it to design functional proteins and evaluate their usefulness. The software could assign both consensus and correlation residues of target proteins. We generated three protein sequences with S -selective hydroxynitrile lyase ( S -HNL) activity, which we call designed S -HNLs; these proteins folded as efficiently as the native S -HNL. Sequence and biochemical analysis of the designed S -HNLs suggested that accumulation of neutral mutations occurs during the process of S -HNLs evolution from a low-activity form to a high-activity (native) form. Taken together, our results demonstrate that our software and the associated methods could be applied not only to design of complete sequences, but also to predictions of protein evolution, especially within families such as esterases and S -HNLs.