Structural aspects of protein-DNA interactions as revealed by conversion of the interacting protein into a sequence-specific cross-linking agent or a chemical nuclease.
Bastia
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Department of Microbiology, Duke University Medical Center, Durham, NC 27710, USA.
D000098:Acetophenones / Q000378:metabolism; D001391:Azo Compounds / Q000378:metabolism; D001426:Bacterial Proteins; D001665:Binding Sites / Q000235:genetics; D003432:Cross-Linking Reagents / Q000378:metabolism; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D004492:Edetic Acid / Q000378:metabolism; D005296:Ferrous Compounds / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D010618:Phenanthrolines / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014466:Ultraviolet Rays
D000098:Acetophenones; D001391:Azo Compounds; D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D004268:DNA-Binding Proteins; D005296:Ferrous Compounds; D010618:Phenanthrolines; C063112:rtP protein, Bacillus subtilis; C055526:Fe(II)-EDTA; D004247:DNA; D004492:Edetic Acid; C025205:1,10-phenanthroline