This study analyzed and predicted following aspects of isopentenyl py- rophosphate isomerases （IPIs） of five north medicinal plants using bioinformatics methods and tools： physical and chemical properties, hydropho...This study analyzed and predicted following aspects of isopentenyl py- rophosphate isomerases （IPIs） of five north medicinal plants using bioinformatics methods and tools： physical and chemical properties, hydrophobicity/hydrophilicity, trans-membrane domain, secondary structure, subcellular localization and so on. The results showed that： there was no notable difference among the physical and chem- ical properties of IPIs of the five north medicinal plants; the IPIs were mainly hy- drophilic; the IPIs were mainly located in chloroplasts by subcellular localization; serine phosphorylation sites were the most; the secondary structures mainly consist- ed of c^-helixes and random coils; no signal peptide existed, indicating that the pro- tein IPI was non-secreted protein; no trans-membrane domain existed; and one functional domain was shown, Le., Nudix Hydrolase Superfamily. This study is of great significance to research on IPI gene functions, deep research on north medic- inal plants, improvement of efficacy of north medicinal plants and rational develop- ment and utilization of medicinal plant resources.展开更多
基金Supported by Science and Technology Planning Project of Mudanjiang(G2015d1974)Funding Project of Training of Famous Teachers in Mudanjiang Normal University(2014QNGG1805)~~
文摘This study analyzed and predicted following aspects of isopentenyl py- rophosphate isomerases （IPIs） of five north medicinal plants using bioinformatics methods and tools： physical and chemical properties, hydrophobicity/hydrophilicity, trans-membrane domain, secondary structure, subcellular localization and so on. The results showed that： there was no notable difference among the physical and chem- ical properties of IPIs of the five north medicinal plants; the IPIs were mainly hy- drophilic; the IPIs were mainly located in chloroplasts by subcellular localization; serine phosphorylation sites were the most; the secondary structures mainly consist- ed of c^-helixes and random coils; no signal peptide existed, indicating that the pro- tein IPI was non-secreted protein; no trans-membrane domain existed; and one functional domain was shown, Le., Nudix Hydrolase Superfamily. This study is of great significance to research on IPI gene functions, deep research on north medic- inal plants, improvement of efficacy of north medicinal plants and rational develop- ment and utilization of medicinal plant resources.
