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Title: Protein surface and core dynamics show concerted hydration-dependent activation
Authors: Wood, K
Gallat, FX
Otten, R
van Heel, AJ
Lethier, M
van Eijck, L
Moulin, M
Haertlein, M
Weik, M
Mulder, FAA
Keywords: Hydration
Neutron spectroscopy
Enzyme activity
Issue Date: 1-Jan-2013
Publisher: Wiley-V C H Verlag GMBH
Citation: Wood, K., Gallat, F. X., Otten, R., van Heel, A. J., Lethier, M., van Eijck, L., Moulin, M., Haertlein, M., Weik, M., & Mulder, F. A. A. (2013). Protein surface and core dynamics show concerted hydration-dependent activation. Angewandte Chemie International Edition, 52(2), 665-668. doi:10.1002/anie.201205898
Abstract: By specifically labeling leucine/valine methyl groups and lysine side chains “inside” and “outside” dynamics of proteins on the nanosecond timescale are compared using neutron scattering (see picture). Surprisingly, both groups display similar dynamics as a function of temperature, and the buried hydrophobic core is sensitive to hydration and undergoes a dynamical transition. © 2013, Wiley-VCH Verlag GmbH & Co. KGaA
Gov't Doc #: 4752
ISSN: 1433-7851
Appears in Collections:Journal Articles

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