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Efficient Isotope Editing of Proteins for Site-Directed Vibrational Spectroscopy
University of Gothenburg, Gothenburg, Sweden.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Organic Chemistry.ORCID iD: 0000-0003-3798-3322
University of Gothenburg, Gothenburg, Sweden.
University of Gothenburg, Gothenburg, Sweden.
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2016 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 138, no 7, p. 2312-2318Article in journal (Refereed) Published
Abstract [en]

Vibrational spectra contain unique information on protein structure and dynamics. However, this information is often obscured by spectral congestion, and site-selective information is not available. In principle, sites of interest can be spectrally identified by isotope shifts, but site-specific isotope labeling of proteins is today possible only for favorable amino acids or with prohibitively low yields. Here we present an efficient cell-free expression system for the site-specific incorporation of any isotope-labeled amino acid into proteins. We synthesized 1.6 mg of green fluorescent protein with an isotope-labeled tyrosine from 100 mL of cell-free reaction extract. We unambiguously identified spectral features of the tyrosine in the fingerprint region of the time-resolved infrared absorption spectra. Kinetic analysis confirmed the existence of an intermediate state between photoexcitation and proton transfer that lives for 3 ps. Our method lifts vibrational spectroscopy of proteins to a higher level of structural specificity.

Place, publisher, year, edition, pages
2016. Vol. 138, no 7, p. 2312-2318
National Category
Biochemistry and Molecular Biology Organic Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-346686DOI: 10.1021/jacs.5b12680PubMedID: 26796542OAI: oai:DiVA.org:uu-346686DiVA, id: diva2:1191834
Available from: 2018-03-20 Created: 2018-03-20 Last updated: 2018-04-11Bibliographically approved

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