Ontology highlight
ABSTRACT:
SUBMITTER: Li P
PROVIDER: S-EPMC6152017 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature

Li Pengyu P Du Shanshan S Li Yang Y He Junlin J
Molecules (Basel, Switzerland) 20170622 7
In the 15-mer catalytic core of 10-23 DNAzyme, each residue contributes to the catalytic conformation differently. Here, the critically conserved T4 and the least conserved T8 were modified on their 5-position with hydroxyl, imidazolyl, and amino groups with a hydrogen-bonding ability. These external functional groups induced new interactions within the catalytic core, resulting in both negative and positive effects on the catalytic activity of 10-23 DNAzyme, and the different linkages could be ...[more]