ISIS Neutron and Muon Source Data Journal

Dissecting the molecular mechanisms of protecting and denaturing osmolytes on protein stability.

Abstract: Extreme environments place severe physicochemical constraints on biological systems and significant perturbations to water.Biological organisms have adapted to environmental niches through a number of mechanisms. One important strategy involves the accumulation of organic solutes in the cell. Of particular interest to our group are the small organic molecules trimethylamine-N-oxide (TMAO) and urea. With NIMROD?s increased flux and developments in structural refinement we are now ideally placed to explore this fascinating system. Our aim is to study the hydration and association of a simple tri-peptide in binary and tertiary solutions of TMAO, urea and water. This will allows us to reveal the molecular mechanisms of protein (de)stabilisation of these important co-solutes, including determining if urea?s affinity for the tri-peptide is reduced in the presence of TMAO.

Local Contact: Dr Tom Headen
Experimenter: Dr Harrison Laurent
Experimenter: Mr Nasralla Nasralla
Experimenter: Professor Lorna Dougan

DOI: 10.5286/ISIS.E.RB2210202

ISIS Experiment Number: RB2210202

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Tom Headen et al; (2022): Dissecting the molecular mechanisms of protecting and denaturing osmolytes on protein stability., STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB2210202

Data is released under the CC-BY-4.0 license.