Comparison of experimental and theoretical data on hydrogen-deuterium exchange for ten globular proteins |
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Authors: | M Yu Suvorina A K Surin N V Dovidchenko M Yu Lobanov O V Galzitskaya |
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Institution: | (1) Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA, 02115–5000, USA; |
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Abstract: | The number of protons available for hydrogen-deuterium exchange was predicted for ten globular proteins using a method described
elsewhere by the authors. The average number of protons replaced by deuterium was also determined by mass spectrometry of
the intact proteins in their native conformations. Based on these data, we find that two models proposed earlier agree with
each other in estimation of the number of protons replaced by deuterium. Using a model with a probability scale for hydrogen
bond formation, we estimated a number of protons replaced by deuterium that is close to the experimental data for long-term
incubation in D2O (24 h). Using a model based on estimations with a scale of the expected number of contacts in globular proteins there is
better agreement with the experimental data obtained for a short period of incubation in D2O (15 min). Therefore, the former model determines weakly fluctuating parts of a protein that are in contact with solvent
only for a small fraction of the time. The latter model (based on the scale of expected number of contacts) predicts either
flexible parts of a protein chain exposed to interactions with solvent or disordered parts of the protein. |
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