title: The relation between mRNA folding and protein structure.
abstract: About 200 mRNA sequences of Escherichia coli and human with matching protein secondary structure data were studied. The mRNA folding for each native sequence and for corresponding randomized sequences was calculated through free energy minimization. We have found that the folding energy of mRNA segments in different protein secondary structures is significantly different. The average Z score is more negative for regular secondary structure (alpha-helix and beta-strand) than that for coil. This suggests that the codon choice in native mRNA sequence coding for protein regular structure contributes more to the mRNA folding stability.
authors.affiliation: Laboratory of Theoretical Biophysics, Faculty of Science and Technology, Inner Mongolia University, Hohhot 010021, China.
authors.forename: Mengwen
authors.initials: M
authors.lastname: Jia
authors.forename: Liaofu
authors.initials: L
authors.lastname: Luo
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry; D006801:Humans; D009690:Nucleic Acid Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012329:RNA, Bacterial / Q000737:chemistry; D012333:RNA, Messenger / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D029968:Escherichia coli Proteins; D011506:Proteins; D012329:RNA, Bacterial; D012333:RNA, Messenger