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Measurement of Submillisecond Protein Folding Using Trp Fluorescence and Photochemical Oxidation

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Protein Folding

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2376))

Abstract

Observation of protein folding on submillisecond time scales requires specialized ultra-rapid mixers coupled to optical or chemical probes. Here we describe the protocol for employing a microfabricated mixer with a mixing time of 8 μs coupled to a UV confocal microscope. This instrument can detect Trp fluorescence and also excite hydroxyl radicals that label the folding protein which can be detected by mass spectrometry.

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Correspondence to Lisa J. Lapidus .

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Witalka, D., Lapidus, L.J. (2022). Measurement of Submillisecond Protein Folding Using Trp Fluorescence and Photochemical Oxidation. In: Muñoz, V. (eds) Protein Folding. Methods in Molecular Biology, vol 2376. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1716-8_7

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  • DOI: https://doi.org/10.1007/978-1-0716-1716-8_7

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1715-1

  • Online ISBN: 978-1-0716-1716-8

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