Proton NMR aromatic spectrum of the operator binding domain of the .lambda. repressor: resonance assignment with application to structure and dynamics
- 1 February 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 26 (3) , 890-897
- https://doi.org/10.1021/bi00377a033
Abstract
The aromatic 1H NMR resonances of the operator binding domain of .lambda. repressor are completely assigned. Since the resonances of this 23-kilodalton domain are too broad for the application of two-dimensional strategies for sequence-specific assignment, an alternative approach has been used. Assignments are obtained by a combination of one- and two-dimensional NMR methods, by the study of genetically altered domains, and by the biosynthetic incorporation of deuterium labels. The resulting assignments provide sensitive markers for tertiary and quaternary structure. Nuclear Overhauser enhancements demonstrate that the major features of the crystal structure, including the dimer contacts, are retained in solution. The rates of aromatic ring rotation indicate that the globular domain is not rigid; significant barriers to ring rotation are observed only in the dimer contact.This publication has 18 references indexed in Scilit:
- Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.Proceedings of the National Academy of Sciences, 1983
- The operator-binding domain of λ repressor: structure and DNA recognitionNature, 1982
- Fluctuations and averaging of proton chemical shifts in the bovine pancreatic trypsin inhibitorBiochemistry, 1982
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectraJournal of Molecular Biology, 1982
- Genetic assignment of resonances in the NMR spectrum of a protein: lac repressor.Proceedings of the National Academy of Sciences, 1981
- Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solutionBiochemistry, 1980
- Regulatory functions of the λ repressor reside in the amino-terminal domainNature, 1979
- The lambda repressor contains two domains.Proceedings of the National Academy of Sciences, 1979
- Differential mobility of the N-terminal headpiece in the lac-repressor proteinJournal of Molecular Biology, 1979
- Primary structure of the λ repressorBiochemistry, 1978