ISIS Neutron and Muon Source Data Journal

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

Abstract: 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

Principal Investigator: Dr Mark Telling
Experimenter: Dr Victoria Garcia Sakai
Experimenter: Dr Stephen Cottrell
Experimenter: Dr David Scott

DOI: 10.5286/ISIS.E.RB1720063

ISIS Experiment Number: RB1720063

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 Mark Telling et al; (2018): How complex is complex: an ALC study of a 10-mer helical peptide chain, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1720063

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