An NMR study on the structure of OR3 in the lambda cro-OR3 complex.
1H-NMR spectra of lambda-OR3 17mer in the complex with lambda-cro has been analysed and the change in its conformation on the complexation has been deduced. The changed conformation is retained until the duplex melts above 55 degrees C. Increase in heat stability of the cro dimer was observed. The result was compared with those of other DNA fragments phi 80-OR2 19 mer and the CRP binding site 22mer mixed with lambda-cro.
D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000235:genetics*; D001483:Base Sequence; D004268:DNA-Binding Proteins; D004926:Escherichia coli / Q000235:genetics*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009690:Nucleic Acid Conformation; D009843:Oligoribonucleotides / Q000378:metabolism*; D011487:Protein Conformation; D012097:Repressor Proteins / Q000378:metabolism; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins
D004268:DNA-Binding Proteins; D009843:Oligoribonucleotides; D012097:Repressor Proteins; D014764:Viral Proteins; D054334:Viral Regulatory and Accessory Proteins; C016649:phage repressor proteins