ArticleBiophysical journal1993
Protein rotational dynamics investigated with a dual EPR/optical molecular probe. Spin-labeled eosin.
Article in Biophysical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- The role of memory-dependent friction and solvent viscosity in isomerization kinetics in viscogenic media.Nature communications · 2024Article
- Molecular Rotational Correlation Times and Nanoviscosity Determined byChemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Perchlorinated Triarylmethyl Radical 99% EnrichedThe journal of physical chemistry. B · 2021Article
- AAngewandte Chemie (International ed. in English) · 2020Article
- Flexibility of the cytoplasmic domain of the anion exchange protein, band 3, in human erythrocytes.Biophysical journal · 2001Article
- The orientation of eosin-5-maleimide on human erythrocyte band 3 measured by fluorescence polarization microscopy.Biophysical journal · 1996Article
- Metal-ligand complexes as a new class of long-lived fluorophores for protein hydrodynamics.Biophysical journal · 1995Article
- Measurement of rotational dynamics by the simultaneous nonlinear analysis of optical and EPR data.Biophysical journal · 1993Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
An acyl spin-label derivative of 5-aminoeosin (5-SLE) was chemically synthesized and employed in studies of rotational dynamics of the free probe and of the probe when bound noncovalently to bovine serum albumin using the spectroscopic techniques of fluorescence anisotropy decay and electron paramagnetic resonance (EPR) and their long-lifetime counterparts phosphorescence anisotropy decay and saturation transfer EPR. Previous work (Beth, A. H., Cobb, C. E., and J. M. Beechem, 1992. Synthesis and characterization of a combined fluorescence, phosphorescence, and electron paramagnetic resonance probe. Society of Photo-Optical Instrumentation Engineers. Time-Resolved Laser Spectroscopy III. 504-512) has shown that the spin-label moiety only slightly altered the fluorescence and phosphorescence lifetimes and quantum yields of 5-SLE when compared with 5-SLE whose nitroxide had been reduced with ascorbate and with the diamagnetic homolog 5-acetyleosin. In the present work, we have utilized time-resolved fluorescence anisotropy decay and linear EPR spectroscopies to observe and quantitate the psec motions of 5-SLE in solution and the nsec motions of the 5-SLE-bovine serum albumin complex. Time-resolved phosphorescence anisotropy decay and saturation transfer EPR studies have been carried out to observe and quantitate the microseconds motions of the 5-SLE-albumin complex in glycerol/buffer solutions of varying viscosity. These latter studies have enabled a rigorous comparison of rotational correlation times obtained from these complementary techniques to be made with a single probe. The studies described demonstrate that it is possible to employ a single molecular probe to carry out the full range of fluorescence, phosphorescence, EPR, and saturation transfer EPR studies. It is anticipated that "dual" molecular probes of this general type will significantly enhance capabilities for extracting dynamics and structural information from macromolecules and their functional assemblies.
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