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Differential mobility of the N-terminal headpiece in the lac-repressor protein.
Authors:N Wade-Jardetzky  R P Bray  W W Conover  O Jardetzky  N Geisler  K Weber
Institution:Stanford Magnetic Resonance Laboratory Stanford University Stanford, CA 94305. U.S.A.;Max-Planck-Institut für Biophysikalische Chemic 3400 Göttingen, West Germany
Abstract:It is shown by resolution enhancement and relaxation studies of the 360 MHz 1H nuclear magnetic resonance spectra of the lac-repressor of Escherichia coli and the two fragments derived from it by limited tryptic digestion (the N-terminal headpiece and remaining T-core) that the majority of the relatively mobile residues in the intact lac-repressor are located in the headpiece. Although nuclear magnetic resonance data clearly indicate that the headpiece is a highly structured entity, even when isolated, it is a more mobile part of the repressor than the T-core.
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