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How does tendency to adopt different secondary structures from antimicrobial lipopeptides affect their membrane binding?
Abstract: This work aims to exploit the unique capability of neutron reflection to examine how 2 antimicrobial lipopeptides that tend to adopt different secondary structures bind to model lipid membranes. Such structural features are sparsely available but are crucial to understanding how different antimicrobial peptides kill different microorganisms through membrane disruptions. Neutron reflection is about the only technique that can unravel the structural features that help us to distinguish the two antimicrobial peptides and link such structural information to antimicrobial behaviour. We request 4 days on Surf to complete this work.
Principal Investigator: Professor Jian Lu
Local Contact: Dr Mario Campana
Experimenter: Mr KE FA
Experimenter: Dr Mingrui Liao
Experimenter: Mr Haoning Gong
Experimenter: Mr kangcheng shen
DOI: 10.5286/ISIS.E.RB1910072
ISIS Experiment Number: RB1910072
Part DOI | Instrument | Public release date | Download Link |
---|---|---|---|
10.5286/ISIS.E.RB1910072-1 | SURF | 03 July 2022 | Download |
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],
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For Example:
Professor Jian Lu et al; (2019): How does tendency to adopt different secondary structures from antimicrobial lipopeptides affect their membrane binding? , STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1910072
Data is released under the CC-BY-4.0 license.