ArticleThe journal of physical chemistry. B2012
Exploring structural and optical properties of fluorescent proteins by squeezing: modeling high-pressure effects on the mStrawberry and mCherry red fluorescent proteins.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Mapping functional dynamics hotspots for protein engineering with NMR peak intensity analysis.Protein engineering, design & selection : PEDS · 2026Article
- Structure, Function and Dynamics of mCoral, a pH-Responsive Engineered Variant of the mCherry Fluorescent Protein with Improved Hydrogen Peroxide Tolerance.International journal of molecular sciences · 2025Article
- Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions.Molecules (Basel, Switzerland) · 2022Review
- pH-dependent transient conformational states control optical properties in cyan fluorescent protein.Journal of the American Chemical Society · 2015Article
- Molecular dynamics simulations of the Nip7 proteins from the marine deep- and shallow-water Pyrococcus species.BMC structural biology · 2014Article
- Chromophore photoreduction in red fluorescent proteins is responsible for bleaching and phototoxicity.The journal of physical chemistry. B · 2014Article
- UV-vis absorption spectrum of a novel Ru(II) complex intercalated in DNA: [Ru(2,2'-bipy)(dppz)(2,2'-ArPy)]⁺.Journal of molecular modeling · 2014Article
- Pressure-induced changes in the fluorescence behavior of red fluorescent proteins.The journal of physical chemistry. B · 2012Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Molecular dynamics calculations of pressure effects on mStrawberry and mCherry fluorescent proteins are reported. The simulations reveal that mStrawberry has much floppier structure at atmospheric pressure, as evidenced by larger backbone fluctuations and the coexistence of two conformers that differ by Ser146 orientation. Consequently, pressure increase has a larger effect on mStrawberry, making its structure more rigid and reducing the population of one of the conformers. The most significant effect of pressure increase is in the hydrogen-bonding network between the chromophore and the nearby residues. The quantum-mechanics/molecular mechanics calculations of excitation energies in mStrawberry explain the observed blue shift and identify Lys70 as the residue that has the most pronounced effect on the spectra. The results suggest that pressure increase causes an initial increase of fluorescence yield only for relatively floppy fluorescent proteins, whereas the fluorescent proteins that have more rigid structures have quantum yields close to their maximum. The results suggest that a low quantum yield in fluorescent proteins is dynamic in nature and depends on the range of thermal motions of the chromophore and fluctuations in the H-bonding network rather than on their average structure.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.