A piece of the puzzle to understand the structure-function relationship of antimicrobial peptides

DOI

The aim of this project is to study the structure of intrinsically disordered antimicrobial peptides under solution conditions and their interactions with surfaces. As model peptides, Melittin and LL37, will be used. The results obtained in this project will be used to develop atomistic and coarse-grained models to be solved with molecular dynamics and Monte Carlo simulations. The goal is to achieve an understanding of the underlying physics on the molecular level, and to decipher the structure-function relationship with respect to sequence determinants. The measurements we aim to perform here are a part of the post doc project by Jenny Andersson and the PhD-project by Mona Koder Hamid, whose projects are a part of a larger project in Skepö research group: Intrinsically disordered proteins: From bulk solution to interaction with surfaces.

Identifier
DOI https://doi.org/10.15151/ESRF-ES-515918997
Metadata Access https://icatplus.esrf.fr/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatplus.esrf.fr:inv/515918997
Provenance
Creator Mona KODER HAMID ORCID logo; Mark TULLY ORCID logo; Marie SKEPO; Amanda ERIKSSON SKOG
Publisher ESRF (European Synchrotron Radiation Facility)
Publication Year 2024
Rights CC-BY-4.0; https://creativecommons.org/licenses/by/4.0
OpenAccess true
Representation
Resource Type Data from large facility measurement; Collection
Discipline Particles, Nuclei and Fields