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Fast slow folding of an outer membrane porin. 2022

Eve E Weatherill, and Monifa A Fahie, and David P Marshall, and Rachel A Andvig, and Matthew R Cheetham, and Min Chen, and Mark I Wallace
Department of Chemistry, King's College London, London SE1 1DB, United Kingdom.

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 (<20 ms), occurring immediately upon arrival at the membrane. This combination of infrequent, but rapid, folding resolves this apparent dichotomy between slow ensemble kinetics and the typical timescales of biomolecular folding.

UI MeSH Term Description Entries
D000072757 Protein Conformation, beta-Strand A secondary structure of proteins where the amino (N-H) groups of a polypeptide backbone, three to ten amino acids in length, establish hydrogen bonds with the carbonyl (C Protein Conformation, beta-Sheet,beta-Pleated Sheet,beta-Sheet,beta-Sheets,beta-Strand,beta-Stranded Structures,beta-Strands,Conformation, beta-Sheet Protein,Conformation, beta-Strand Protein,Conformations, beta-Sheet Protein,Conformations, beta-Strand Protein,Protein Conformation, beta Sheet,Protein Conformation, beta Strand,Protein Conformations, beta-Sheet,Protein Conformations, beta-Strand,Sheet, beta-Pleated,Sheets, beta-Pleated,beta Pleated Sheet,beta Sheet,beta Sheets,beta Strand,beta Stranded Structures,beta Strands,beta-Pleated Sheets,beta-Sheet Protein Conformation,beta-Sheet Protein Conformations,beta-Strand Protein Conformation,beta-Strand Protein Conformations,beta-Stranded Structure
D000072760 Single Molecule Imaging High resolution imaging techniques that allow visualization of individual molecules of proteins, lipids, or nucleic acids within cells or tissues. Single Molecule Analysis,Single Molecule Tracking,Single Particle Analysis,Single Particle Imaging,Single Particle Microscopy,Single Particle Spectroscopy,Single Particle Tracking,Single Molecule Microscopy,Single Molecule Spectroscopy,Analyses, Single Particle,Analysis, Single Molecule,Analysis, Single Particle,Imaging, Single Molecule,Imaging, Single Particle,Microscopies, Single Particle,Microscopy, Single Molecule,Microscopy, Single Particle,Particle Tracking, Single,Single Molecule Analyses,Single Particle Analyses,Single Particle Microscopies,Single Particle Spectroscopies,Single Particle Trackings,Spectroscopy, Single Molecule,Spectroscopy, Single Particle,Tracking, Single Molecule,Tracking, Single Particle
D001425 Bacterial Outer Membrane Proteins Proteins isolated from the outer membrane of Gram-negative bacteria. OMP Proteins,Outer Membrane Proteins, Bacterial,Outer Membrane Lipoproteins, Bacterial
D017510 Protein Folding Processes involved in the formation of TERTIARY PROTEIN STRUCTURE. Protein Folding, Globular,Folding, Globular Protein,Folding, Protein,Foldings, Globular Protein,Foldings, Protein,Globular Protein Folding,Globular Protein Foldings,Protein Foldings,Protein Foldings, Globular
D018272 Porins Porins are protein molecules that were originally found in the outer membrane of GRAM-NEGATIVE BACTERIA and that form multi-meric channels for the passive DIFFUSION of WATER; IONS; or other small molecules. Porins are present in bacterial CELL WALLS, as well as in plant, fungal, mammalian and other vertebrate CELL MEMBRANES and MITOCHONDRIAL MEMBRANES. Pore Protein,Pore Proteins,Porin,Protein, Pore,Proteins, Pore
D029968 Escherichia coli Proteins Proteins obtained from ESCHERICHIA COLI. E coli Proteins
D031541 Fluorescence Resonance Energy Transfer A type of FLUORESCENCE SPECTROSCOPY using two FLUORESCENT DYES with overlapping emission and absorption spectra, which is used to indicate proximity of labeled molecules. This technique is useful for studying interactions of molecules and PROTEIN FOLDING. Forster Resonance Energy Transfer

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