Mirror-image polymerase chain reaction

Sulfolobus solfataricus
DOI: 10.1038/celldisc.2017.37 Publication Date: 2017-10-17T09:21:17Z
ABSTRACT
The construction of mirror-image biological systems may open the next frontier for biomedical technology development and discovery. Here we have designed chemically synthesized a mutant version thermostable Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) consisting d-amino acids. With total peptide length 358 amino acid residues, it is largest protein reported to date. We show that d-polymerase able amplify 120-bp l-DNA sequence coding Escherichia coli 5S ribosomal RNA gene rrfB by chain reaction, both natural operate with strict chiral specificity. efficient miPCR lead many practical applications, such as systematic evolution ligands exponential enrichment selection therapeutically promising nuclease-resistant l-nucleic aptamers.
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