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The dynamical transition in dry proteins?
Abstract: Water plays a critical role in determining the structure and function of biological system. A hydration level, h~0.2 g water/g protein, is often found to be the minimum requirement for the dynamical transition in protein at ~200K. However, we have demonstrated that dry proteins also present a dynamical transition around 200 K if measured in the perdeuterated state by neutron scattering. This transition is absent in the dry hydrogenated protein due to the strong contribution of methyl rotations. Our results suggest that, as long as one can remove the contribution from methyl motions, the dynamical transition will be evident in the dry state. Using a neutron instrument with a low energy resolution such that methyl rotations cannot be resolved, e.g., ~100ueV, such as OSIRIS with PG004 reflection will assist us in analyzing the origin and influence of this dynamical transition in dry state.
Principal Investigator: Professor liang hong
Experimenter: Mr Zhuo Liu
Experimenter: Dr Victoria Garcia Sakai
Experimenter: Dr Chenxing Yang
DOI: 10.5286/ISIS.E.RB1810096
ISIS Experiment Number: RB1810096
Part DOI | Instrument | Public release date | Download Link |
---|---|---|---|
10.5286/ISIS.E.90582867 | OSIRIS | 25 March 2021 | Download |
- | IRIS | 27 April 2021 | Download |
Publisher: STFC ISIS Neutron and Muon Source
Data format: RAW/Nexus
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Data Citation
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[author], [date], [title], [publisher],
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Professor liang hong et al; (2018): The dynamical transition in dry proteins?, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1810096
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