title: Hydrogen exchange of individual amide protons in the E. coli lac repressor DNA-binding domain: a nuclear magnetic resonance study.
abstract: Proton exchange in lac repressor headpiece was studied by COSY and 2D NOE spectroscopy. The exchange rates of amide protons, stabilized by the hydrogen bonds of the three alpha-helices of the headpiece, could be determined quantitatively. The exchange rates in these helices showed repetitive patterns of about three to four residues. A correlation with the position of the amide proton in the interior or the exterior of the alpha-helix of the protein was found. The exchange data strongly support the validity of the three-dimensional structure, as determined recently (Kaptein, R. et al., J. Mol. Biol. 182, 179-182 (1985)).
authors.affiliation: Department of Physical Chemistry, University of Groningen, The Netherlands.
authors.forename: R
authors.initials: R
authors.lastname: Boelens
authors.forename: P
authors.initials: P
authors.lastname: Gros
authors.forename: R M
authors.initials: RM
authors.lastname: Scheek
authors.forename: J A
authors.initials: JA
authors.lastname: Verpoorte
authors.forename: R
authors.initials: R
authors.lastname: Kaptein
mesh_terms: D004268:DNA-Binding Proteins; D004926:Escherichia coli; D007474:Ion Exchange; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D011487:Protein Conformation; D011522:Protons; D012097:Repressor Proteins; D014157:Transcription Factors
chemical_list: D004268:DNA-Binding Proteins; D011522:Protons; D012097:Repressor Proteins; D014157:Transcription Factors