Abstract
The amide proton magnetic resonances of the λ-cro repressor protein have been examined. In order to assign them to specific amino acid residues, we labeled the cro protein by incorporating15N-enriched leucine or 15N-enriched lysine and then conducted 1H/15N heteronuclear multiquantum coherence (HMQC) spectroscopy of the labeled cro protein. The chemical shifts of the amide proton resonances were titrated by the addition of operator DNA fragments. From the behavior of the shifts on binding to the operator DNAs, the DNA binding surface of the cro protein has been deduced. On the basis of the results with DNAs with different base sequences, the origins of the specific and nonspecific interactions are discussed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
