Hydrogen exchange of individual amide protons in the E. coli lac repressor DNA-binding domain: a nuclear magnetic resonance study.
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)).
Boelens
R
R
Department of Physical Chemistry, University of Groningen, The Netherlands.
Gros
P
P
Scheek
R M
RM
Verpoorte
J A
JA
Kaptein
R
R
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
D004268:DNA-Binding Proteins; D011522:Protons; D012097:Repressor Proteins; D014157:Transcription Factors