{"entity": "publication", "iuid": "13a57ee6a62a4403941ceda399b774f8", "timestamp": "2026-09-12T20:32:09.741Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/13a57ee6a62a4403941ceda399b774f8.json"}, "display": {"href": "https://publications.scilifelab.se/publication/13a57ee6a62a4403941ceda399b774f8"}}, "title": "Efficient Isotope Editing of Proteins for Site-Directed Vibrational Spectroscopy.", "authors": [{"family": "Peuker", "given": "Sebastian", "initials": "S"}, {"family": "Andersson", "given": "Hanna", "initials": "H"}, {"family": "Gustavsson", "given": "Emil", "initials": "E"}, {"family": "Maiti", "given": "Kiran Sankar", "initials": "KS"}, {"family": "Kania", "given": "Rafal", "initials": "R"}, {"family": "Karim", "given": "Alavi", "initials": "A"}, {"family": "Niebling", "given": "Stephan", "initials": "S"}, {"family": "Pedersen", "given": "Anders", "initials": "A"}, {"family": "Erdelyi", "given": "Mate", "initials": "M"}, {"family": "Westenhoff", "given": "Sebastian", "initials": "S"}], "type": "journal article", "published": "2016-02-24", "journal": {"volume": "138", "issn": "1520-5126", "issue": "7", "pages": "2312-2318", "title": "J. Am. Chem. Soc.", "issn-l": "0002-7863"}, "abstract": "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.", "doi": "10.1021/jacs.5b12680", "pmid": "26796542", "labels": {"Swedish NMR Centre": "Collaborative"}, "xrefs": [], "notes": [], "created": "2017-05-03T13:02:49.193Z", "modified": "2025-10-17T13:04:00.668Z"}