Fast slow folding of an outer membrane porin

Autor:	Eve E. Weatherill, Monifa A. Fahie, David P. Marshall, Rachel A. Andvig, Matthew R. Cheetham, Min Chen, Mark I. Wallace
Rok vydání:	2022
Předmět:	Protein Folding Multidisciplinary Escherichia coli Proteins Fluorescence Resonance Energy Transfer Porins Protein Conformation beta-Strand Single Molecule Imaging Bacterial Outer Membrane Proteins
Zdroj:	Weatherill, E E, Fahie, M A, Marshall, D P, Andvig, R A, Cheetham, M R, Chen, M & Wallace, M I 2022, ' Fast slow folding of an outer membrane porin ', Proceedings of the National Academy of Sciences, vol. 119, no. 20, e2121487119 . https://doi.org/10.1073/pnas.2121487119
ISSN:	1091-6490
DOI:	10.1073/pnas.2121487119
Popis:	In comparison to globular proteins, the spontaneous folding and insertion of β-barrel membrane proteins are surprisingly slow, typically occurring on the order of minutes. Using single-molecule Förster resonance energy transfer to report on the folding of fluorescently labeled outer membrane protein G we measured the real-time insertion of a β-barrel membrane protein from an unfolded state. Folding events were rare and fast (
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::143ffc6e0253e019ed0ad48c3ceab0c6 https://pubmed.ncbi.nlm.nih.gov/35549548 Zobrazit plný text záznamu