Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide

Antimicrobial peptides (AMPs) selectively form pores in microbial membranes in process not fully understood. Here the authors use experimentally guided molecular dynamics to study maculatin pore formation, showing how this AMP assembles into transient and structurally diverse oligomeric pores in cel...

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Autores principales: Yukun Wang, Charles H. Chen, Dan Hu, Martin B. Ulmschneider, Jakob P. Ulmschneider
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/322f5d07a3e6460aa7ea543a7dc9effb
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spelling oai:doaj.org-article:322f5d07a3e6460aa7ea543a7dc9effb2021-12-02T17:33:10ZSpontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide10.1038/ncomms135352041-1723https://doaj.org/article/322f5d07a3e6460aa7ea543a7dc9effb2016-11-01T00:00:00Zhttps://doi.org/10.1038/ncomms13535https://doaj.org/toc/2041-1723Antimicrobial peptides (AMPs) selectively form pores in microbial membranes in process not fully understood. Here the authors use experimentally guided molecular dynamics to study maculatin pore formation, showing how this AMP assembles into transient and structurally diverse oligomeric pores in cell membranes.Yukun WangCharles H. ChenDan HuMartin B. UlmschneiderJakob P. UlmschneiderNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Yukun Wang
Charles H. Chen
Dan Hu
Martin B. Ulmschneider
Jakob P. Ulmschneider
Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
description Antimicrobial peptides (AMPs) selectively form pores in microbial membranes in process not fully understood. Here the authors use experimentally guided molecular dynamics to study maculatin pore formation, showing how this AMP assembles into transient and structurally diverse oligomeric pores in cell membranes.
format article
author Yukun Wang
Charles H. Chen
Dan Hu
Martin B. Ulmschneider
Jakob P. Ulmschneider
author_facet Yukun Wang
Charles H. Chen
Dan Hu
Martin B. Ulmschneider
Jakob P. Ulmschneider
author_sort Yukun Wang
title Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_short Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_full Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_fullStr Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_full_unstemmed Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
title_sort spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/322f5d07a3e6460aa7ea543a7dc9effb
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AT danhu spontaneousformationofstructurallydiversemembranechannelarchitecturesfromasingleantimicrobialpeptide
AT martinbulmschneider spontaneousformationofstructurallydiversemembranechannelarchitecturesfromasingleantimicrobialpeptide
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