PMID: 7019910May 1, 1981Paper

Genetic assignment of resonances in the NMR spectrum of a protein: lac repressor

Proceedings of the National Academy of Sciences of the United States of America
M JaremaJ H Miller

Abstract

By using a systematic genetic approach, the resonances in the 19F NMR spectrum of 3-fluorotyrosine-substituted lac repressor protein have been assigned. The NMR data indicate that each monomer of the repressor consists of two distinct and independent domains. One domain, the NH2-terminal sixth of the primary sequence, which has been shown to be very important for DNA binding, is very mobile. The remaining COOH-terminal sequence is more rigid. Ligands of the repressor, which affect its DNA binding capability, lead to conformational changes in the COOH-terminal domain. The approach to the assignment of spectral features taken here can be extended to other systems.

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Citations

Jun 1, 2011·Journal of Biomolecular NMR·Carlos AmeroJérôme Boisbouvier
Nov 5, 1984·Journal of Molecular Biology·S P Manly, K S Matthews
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May 2, 1983·European Journal of Biochemistry·F BuckW E Hull
Dec 1, 1992·Photochemistry and Photobiology·E S HazardR K Crouch

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