Reversible folding-unfolding and structural study in protein-ionic liquid systems

DOI

It has been recently shown that reversible thermal folding-unfolding, stabilization and high solubility of proteins (e.g. lysozyme) can be achieved when dissolved in protic ionic liquids (e.g. ethylammonium nitrate, EAN).These interesting properties have been so far explored only marginally from the tructural point of view. SANS measurements, complemented by SAXS and DLS ones, can be extremely valuable to explore the nature of the interaction between biomacromolecules and smart new solvents such as ionic liquids.We propsoe to explore the morphology of lysozyme when dissolved in EAN, as a function of concentration and temperature, using the SANS technique and other ancillary measurments.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24088610
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24088610
Provenance
Creator Dr Alessandro Triolo
Publisher ISIS Neutron and Muon Source
Publication Year 2015
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2012-03-06T00:16:53Z
Temporal Coverage End 2012-03-10T09:19:27Z