Comparing peptide folding states in non-aqueous and aqueous solutions

DOI

How proteins fold from their linear sequence into their functional structures is still not understood and the misfolding of proteins is linked to a variety of diseases - such as Alzheimer's, Huntington's and diabetes. In life, proteins fold in aqueous solution and as such investigation of this process must be assessed in a similar environment. This proposal is part of a programme of work to investigate protein folding in solution using small peptides which adopt a range of conformations in solution. This allows for an assessment of hydration in the folded and unfolded states of a peptide allowing for important details of how hydration contributes to this process to be determined.

Identifier
DOI https://doi.org/10.5286/ISIS.E.85068108
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/85068108
Provenance
Creator Dr Sam Callear; Dr Sylvia McLain; Mr Thomas Dixon; Ms Nicola Steinke; Dr Silvia Imberti
Publisher ISIS Neutron and Muon Source
Publication Year 2020
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 Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2017-05-03T08:00:00Z
Temporal Coverage End 2017-05-09T10:32:48Z