Dimerization of the operator binding domain of phage .lambda. repressor

Dimerization of lambda repressor is required for its binding to operator DNA. As part of a continuing study of the structural basis of the coupling between dimer formation and operator binding, we have undertaken 1H NMR and gel filtration studies of the dimerization of the N-terminal domain of lambd...

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Veröffentlicht in:	Biochemistry (Easton) 1987-02, Vol.26 (3), p.897-904
Hauptverfasser:	Weiss, Michael A, Pabo, Carl O, Karplus, Martin, Sauer, Robert T
Format:	Artikel
Sprache:	eng
Schlagworte:	550601 - Medicine- Unsealed Radionuclides in Diagnostics 550602 - Medicine- External Radiation in Diagnostics- (1980-) AMINO ACIDS Amino Acids - analysis BACTERIA Bacteriophage lambda - metabolism BACTERIOPHAGES BARYONS Binding Sites Biological and medical sciences CARBOXYLIC ACIDS CHEMICAL REACTIONS CHROMATOGRAPHY COHERENT SCATTERING DIFFRACTION DIMERIZATION DNA-Binding Proteins ELEMENTARY PARTICLES ESCHERICHIA COLI Escherichia coli - metabolism FERMIONS FILTRATION Fundamental and applied biological sciences. Psychology GENOTYPE HADRONS HYDROXY ACIDS Interactions. Associations Intermolecular phenomena LEUCINE LIQUID COLUMN CHROMATOGRAPHY Macromolecular Substances MAGNETIC RESONANCE Magnetic Resonance Spectroscopy - methods MICROORGANISMS Models, Molecular Molecular biophysics NUCLEAR MAGNETIC RESONANCE NUCLEONS Operon ORGANIC ACIDS ORGANIC COMPOUNDS PARASITES phage lambda POLYMERIZATION Protein Binding Protein Conformation PROTEINS PROTONS RADIOLOGY AND NUCLEAR MEDICINE Repressor Proteins - metabolism repressors RESONANCE SCATTERING SEPARATION PROCESSES SERINE Transcription Factors - metabolism VALINE Viral Proteins Viral Regulatory and Accessory Proteins VIRUSES X-RAY DIFFRACTION
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