Protein surface and core dynamics show concerted hydration-dependent activation
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Date
2013-01-01
Journal Title
Journal ISSN
Volume Title
Publisher
Wiley-V C H Verlag GMBH
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
Description
Keywords
Hydration, Isotopes, Neutron spectroscopy, Proteins, Enzyme activity, Myoglobin, Lysozyme, Glass
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