Fast slow folding of an Outer Membrane Porin
Keyword(s):
AbstractIn comparison to globular proteins, the spontaneous folding and insertion of β-barrel membrane proteins is surprisingly slow, typically occurring on the order of minutes. Using single-molecule Förster Resonance Energy Transfer to report on the folding of fluorescently-labelled 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 rare, folding resolves this apparent dichotomy between slow ensemble kinetics, and the typical timescales of biomolecular folding.
2000 ◽
Vol 104
(21)
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pp. 5171-5178
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2011 ◽
pp. 273-289
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2019 ◽
Vol 10
(11)
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pp. 2849-2856
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