Interactions between cro repressor and the model specific binding site
- 1 October 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 175 (2) , 317-320
- https://doi.org/10.1016/0014-5793(84)80759-0
Abstract
Binding of λ phage cro repressor to the synthetic half of OR3, the most conservative half of the specific binding sites, was investigated by proton nuclear magnetic resonance spectroscopy. It was found that the α-helical segment (27–36) of the protein was involved in specific interactions with the model binding site. The 3-dimensional structure of cro repressor does not change noticeably upon complex formation. Intercalation can be excluded as a possible means of interactionKeywords
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