Hydrogen Exchange of Individual Amide Protons in the E. Coli lac Repressor DNA-binding Domain: A Nuclear Magnetic Resonance Study (29) |
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| Authors: | R. Boelens P. Gros R. M. Scheek J. A. Verpoorte R. Kaptein |
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| Affiliation: | Department of Physical Chemistry , University of Groningen , Nijenborgh 16, 9747 AG , Groningen , The Netherlands |
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| Abstract: | 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 α-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 α-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)). |
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