ArticleJournal of the Royal Society, Interface2023
Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition.
Article in Journal of the Royal Society, Interface, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 9 citations in OpenAlex.
- Indocyanine green excitation-emission matrix characterization: excitation-dependent emission shifts and application-specific spectra.Journal of biomedical optics · 2026Article
- Self-assembling proteins compose the chemically resistant shell biomaterial of planktonic tintinnid ciliates.Nature communications · 2026Article
- Indocyanine green excitation-emission matrix characterization: excitation-dependent emission shifts and application-specific spectra.bioRxiv : the preprint server for biology · 2025Article
- The Lassa Virus Stable Signal Peptide Undergoes a Conformational Change to Aid Viral Fusion.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Novel Benzothiazole Boc-Phe-Phe-Bz Derivative Dipeptide Forming Fluorescent and Nonlinear Optical Self-Assembled Structures.Molecules (Basel, Switzerland) · 2025Article
- Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition.Journal of the Royal Society, Interface · 2023Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Red edge excitation shift (REES) spectroscopy relies on the unique emission profiles of fluorophore-solvent interactions to profile protein molecular dynamics. Recently, we reported the use of REES to compare the stability of 32 polymorphic IgG antibodies natively containing tryptophan reporter fluorophores. Here, we expand on this work to investigate the sensitivity of REES to variations in tryptophan content using a subset of IgG3 antibodies containing arginine to tryptophan polymorphisms. Structural analysis revealed that the additional tryptophan residues were situated in highly solvated environments. Subsequently, REES showed clear differences in fluorescence emission profiles when compared with the unmutated variants, thereby limiting direct comparison of their structural dynamics. These findings highlight the exquisite sensitivity of REES to minor variations in protein structure and tryptophan composition.
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