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5 March 2021 Interrogation of local interactions between tetramethylrhodamine and voltage sensing phosphatase with two-photon absorption polarization ratio and cross section spectra
Mikhail Drobizhev, Wil Ratzan, Susy C. Kohout
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Proceedings Volume 11660, Reporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications XIII; 1166008 (2021) https://doi.org/10.1117/12.2579348
Event: SPIE BiOS, 2021, Online Only
Abstract
Fluorescent dyes, attached to proteins are widely used to study different biological processes. However, physical mechanisms of fluorescence change in response to particular stimuli are poorly understood. Here we use two-photon polarization ratio Omega and cross section spectra to study the nature of local interactions between tetramethyrhodamine-6-maleimide and voltage sensing phosphatase (VSP). We show that when rhodamine binds to VSP, it undergoes a conformational change corresponding to a twist of a dihedral angle between the phenyl and xanthene planes from 90 to 70–80 degree. This change is probably due to steric clashes between the rhodamine and neighbor amino acid residues.
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Mikhail Drobizhev, Wil Ratzan, and Susy C. Kohout "Interrogation of local interactions between tetramethylrhodamine and voltage sensing phosphatase with two-photon absorption polarization ratio and cross section spectra", Proc. SPIE 11660, Reporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications XIII, 1166008 (5 March 2021); https://doi.org/10.1117/12.2579348
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KEYWORDS
Proteins
Polarization
Absorption
Luminescence
Rhodamine
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