NDLI: Comparison of experimental and theoretical data on hydrogen-deuterium exchange for ten globular proteins

Content Provider	Springer Nature Link
Author	Suvorina, M. Yu. Surin, A. K. Dovidchenko, N. V. Lobav, M. Yu. Galzitskaya, O. V.
Copyright Year	2012
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.
Starting Page	616
Ending Page	623
Page Count	8
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	77
Issue Number	6
e-ISSN	16083040
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2012-06-14
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	hydrogen-deuterium exchange structure hydrogen bond mass spectrometry Biomedicine general Biochemistry Microbiology Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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