ATP selection in a random peptide library consisting of prebiotic amino acids
| Autor: | Qingyong Yang, Bai-Xue Chen, Rong Liu, Tian Tian, Xin-Yi Chu, Pengfei Dong, Hong-Yu Zhang, Shou-Kai Kang, Xi-Shuai Jia |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
DNA
Complementary Biophysics Peptide Plasma protein binding Biology Ligands Biochemistry DNA sequencing chemistry.chemical_compound Adenosine Triphosphate Peptide Library Complementary DNA Genomic library RNA Messenger Amino Acids Peptide library Molecular Biology Gene Library Genetics chemistry.chemical_classification Hydrolysis Computational Biology High-Throughput Nucleotide Sequencing Proteins Cell Biology Amino acid Prebiotics chemistry Peptides Adenosine triphosphate Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 466:400-405 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2015.09.038 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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