How complex is complex: an ALC study of a 10-mer helical peptide chain

DOI

There have been ALC studies on the interaction of muons with native proteins, but little systematic work that contributes understanding of how spectroscopic information alters with structure. However, to truly understand the applicability of the ALC method to native material one has tounderstand the limitations of the method in such complex bio-polymers. To test these limits, we wish to build on our phenylalanine study and use a short peptide that forms an alpha-helical structure. Using the sequence, Glu-Leu-Glu-Lys-Glu-Leu-Glu-Lys-Lys-Phe, we expect muonaddition to the Phe ring and C=0 species (backbone) only. By already studying coupling to Phe, we will be able to understand how addition of this acid to a C=O rich sequence alters the Phe resonance, understand the resonance signature from those muons tagging the backbone andmonitor both in the folded and unfolded state

Identifier
DOI https://doi.org/10.5286/ISIS.E.97971287
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/97971287
Provenance
Creator Dr Mark Telling; Dr Victoria Garcia Sakai; Dr Stephen Cottrell; Dr David Scott
Publisher ISIS Neutron and Muon Source
Publication Year 2021
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 2018-09-22T23:00:00Z
Temporal Coverage End 2018-09-26T06:10:17Z