Solution NMR Studies of Intact Lambda Repressor
- 1 October 1983
- journal article
- research article
- Published by Taylor & Francis in Journal of Biomolecular Structure and Dynamics
- Vol. 1 (1) , 151-157
- https://doi.org/10.1080/07391102.1983.10507431
Abstract
Using a combination of two and one-dimensional NMR spectroscopy, it is shown that in the intact bacteriophage lamda repressor, the N-terminal domain assumes the same global structure as when it remains isolated. It is further shown that the N-terminal domain is only loosely attached to the C-terminal domain in the intact repressor.This publication has 23 references indexed in Scilit:
- Repressor structure and the mechanism of positive controlCell, 1983
- Fluctuations and averaging of proton chemical shifts in the bovine pancreatic trypsin inhibitorBiochemistry, 1982
- Lac Repressor: a proton magnetic resonance look at the deoxyribonucleic acid binding fragmentBiochemistry, 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
- Differential mobility of the N-terminal headpiece in the lac-repressor proteinJournal of Molecular Biology, 1979
- 1H NMR study of the lactose repressor from Escherichia coliFEBS Letters, 1978
- Unusual segmental flexibility in a region of tobacco mosaic virus coat proteinNature, 1978
- Primary structure of the λ repressorBiochemistry, 1978
- High Resolution Proton Magnetic Resonance Studies of Fully Deuterated and Isotope Hybrid ProteinsNature, 1969