ArticleThe journal of physical chemistry. B2014
General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins.
Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Synthesis and Application of a Glucoconjugated Organometallic Rhenium Complex as an IR Imaging Probe for Glycolytic Cancer Cells.Molecules (Basel, Switzerland) · 2025Article
- Rational incorporation of any unnatural amino acid into proteins by machine learning on existing experimental proofs.Computational and structural biotechnology journal · 2022Article
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Site-Specific 1D and 2D IR Spectroscopy to Characterize the Conformations and Dynamics of Protein Molecular Recognition.The journal of physical chemistry. B · 2019Article
- Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine.RSC advances · 2018Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Probing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study.Acta crystallographica. Section D, Structural biology · 2016Article
- Azidoethoxyphenylalanine as a Vibrational Reporter and Click Chemistry Partner in Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015Review
- Article
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Authors and funding
8 authors.
Funding
Abstract
A high-sensitivity metal-carbonyl-based IR probe is described that can be incorporated into proteins or other biomolecules in very high yield via Click chemistry. A two-step strategy is demonstrated. First, a methionine auxotroph is used to incorporate the unnatural amino acid azidohomoalanine at high levels. Second, a tricarbonyl (η(5)-cyclopentadienyl) rhenium(I) probe modified with an alkynyl linkage is coupled via the Click reaction. We demonstrate these steps using the C-terminal domain of the ribosomal protein L9 as a model system. An overall incorporation level of 92% was obtained at residue 109, which is a surface-exposed residue. Incorporation of the probe into a surface site is shown not to perturb the stability or structure of the target protein. Metal carbonyls are known to be sensitive to solvation and protein electrostatics through vibrational lifetimes and frequency shifts. We report that the frequencies and lifetimes of this probe also depend on the isotopic composition of the solvent. Comparison of the lifetimes measured in H2O versus D2O provides a probe of solvent accessibility. The metal carbonyl probe reported here provides an easy and robust method to label very large proteins with an amino-acid-specific tag that is both environmentally sensitive and a very strong absorber.
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