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Protein Dynamics in Living Cells

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Related Experiment Video

Updated: Oct 12, 2025

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

Circularly Permuted Far-Red Fluorescent Proteins.

Tianchen Wu¹, Yu Pang^1,2, Hui-Wang Ai^1,2,3

¹Department of Molecular Physiology and Biological Physics, and Center for Membrane and Cell Physiology, University of Virginia School of Medicine, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.

|November 25, 2021

Summary

This summary is machine-generated.

Researchers developed five novel circularly permuted far-red fluorescent proteins (cpFrFPs) for improved in vivo imaging. These engineered proteins offer enhanced tissue penetration and reduced autofluorescence, advancing genetically encoded fluorescent protein indicators.

Keywords:

circular permutation far-red fluorescent protein genetically encoded fluorescent biosensor pH sensitivity

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Last Updated: Oct 12, 2025

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Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

Area of Science:

Biochemistry
Molecular Biology
Biophotonics

Background:

Genetically encoded fluorescent protein indicators (GEFPIs) are crucial tools in biological research.
Expanding the spectral range of GEFPIs, particularly into the far-red region (>600 nm), offers significant advantages for in vivo imaging.

Purpose of the Study:

To explore the feasibility of circular permutation for far-red fluorescent proteins (FPs).
To engineer novel circularly permuted far-red FPs (cpFrFPs) for advanced biological imaging applications.

Main Methods:

Circularly permuting two far-red FPs: mMaroon1 and mCarmine.
Constructing and mutagenizing FP variants based on known circularly permuted topologies.
Screening for fluorescent variants with excitation/emission maxima >600 nm.

Main Results:

Identified five novel cpFrFPs with spectral properties in the far-red range (>600 nm).
Some variants demonstrated good brightness and efficient chromophore maturation.
These cpFrFPs exhibit potential for improved tissue penetration and reduced autofluorescence.

Conclusions:

Circular permutation is a viable strategy for engineering far-red fluorescent proteins.
The developed cpFrFPs serve as promising starting points for creating advanced GEFPIs for in vivo imaging.
These engineered proteins could enhance deep-tissue imaging and reduce phototoxicity.