
doi: 10.1007/bf00309567
pmid: 4473703
The interaction of netropsin with DNA and synthetic polydeoxyribonucleotides was studied by absorption spectrophotometry and circular dichroism. The results are consistent with a model in which a netropsin molecule occupies five base pairs in binding and carries three reaction sites each capable of interacting with one AT base pair. We associate these reaction sites with the antibiotic peptide groups which probably interact with AT base pairs by a hydrogen bonding mechanism.
Binding Sites, Circular Dichroism, Osmolar Concentration, Polynucleotides, DNA Viruses, Molecular Conformation, DNA, Thymus Gland, Coliphages, Anti-Bacterial Agents, Molecular Weight, Kinetics, DNA, Viral, Animals, Nucleic Acid Conformation, Cattle, Spectrophotometry, Ultraviolet, Oligopeptides, Mathematics
Binding Sites, Circular Dichroism, Osmolar Concentration, Polynucleotides, DNA Viruses, Molecular Conformation, DNA, Thymus Gland, Coliphages, Anti-Bacterial Agents, Molecular Weight, Kinetics, DNA, Viral, Animals, Nucleic Acid Conformation, Cattle, Spectrophotometry, Ultraviolet, Oligopeptides, Mathematics
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 81 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 1% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
