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• W1646738685 abstract "Based upon many theoretical findings on protein evolution, we proposed a ligand-selection model for the origin of proteins, in which the most ancient proteins originated from ATP selection in a pool of random peptides. To test this ligand-selection model, we constructed a random peptide library consisting of 15 types of prebiotic amino acids and then used cDNA display to perform six rounds of in vitro selection with ATP. By means of next-generation sequencing, the most prevalent sequence was defined. Biochemical and biophysical characterization of the selected peptide showed that it was stable and foldable and had ATP-hydrolysis activity as well." @default.
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• W1646738685 date "2015-10-01" @default.
• W1646738685 modified "2023-10-18" @default.
• W1646738685 title "ATP selection in a random peptide library consisting of prebiotic amino acids" @default.
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• W1646738685 doi "https://doi.org/10.1016/j.bbrc.2015.09.038" @default.
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