Journal ArticleDOI
On the nanosecond mobility in proteins: Edge excitation fluorescence red shift of protein-bound 2-(p-toluidinylnaphthalene)-6-sulfonate
TLDR
The results of this work strongly support the significant dye fluorescence spectral shifts on protein binding, being determined not only by polarity changes in their environment, but also by relaxation properties of protein groups in this environment.About:
This article is published in Biophysical Chemistry.The article was published on 1982-05-01. It has received 95 citations till now. The article focuses on the topics: Fluorescence spectroscopy & Excited state.read more
Citations
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The red‐edge effects: 30 years of exploration
TL;DR: Red-edge effects were discovered for electron-transfer and proton-transfer reactions if they depended on the dynamics of the environment and stimulated the emergence and development of cryogenic energy-selective and single-molecular techniques that became valuable tools in their own right in chemistry and biophysics research.
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Interplay between excited-state intramolecular proton transfer and charge transfer in flavonols and their use as protein-binding-site fluorescence probes
TL;DR: The utility of DHF as a discriminating fluorescence probe for protein binding sites is suggested by the strong dependence of the charge-transfer fluorescence on polarity of the environment and by various static and dynamic parameters of the Charge-transfer and proton- transfer fluorescence which can be determined.
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Nature of biological water : a femtosecond study
TL;DR: It is shown that the ultrafast (approximately 1 ps) component arises from an extended hydrogen bond network while the ultraslow component originates from binding of a water molecule to a biological macromolecule.
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Femtosecond solvation dynamics in a neat ionic liquid and ionic liquid microemulsion: excitation wavelength dependence.
Aniruddha Adhikari,Kalyanasis Sahu,Shantanu Dey,Subhadip Ghosh,Ujjwal Mandal,Kankan Bhattacharyya +5 more
TL;DR: Solvation dynamics in a neat ionic liquid, 1-pentyl-3-methyl-imidazolium tetra-flouroborate ([pmim][BF4]) and its microemulsion in Triton X-100 (TX-100)/benzene is studied using femtosecond up-conversion.
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Red-edge excitation of fluorescence and dynamic properties of proteins and membranes.
TL;DR: The spectral shifts and lifetime data indicate that red-edge excitation results in the selective excitation of "solvent-relaxed" fluorophores, and comparison of the data obtained for TNS in solvents and bound to the macromolecules may estimate the relaxation rate of the environment.
References
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Journal ArticleDOI
Fluorescent probes for conformational states of proteins. I. Mechanism of fluorescence of 2-p-toluidinylnaphthalene-6-sulfonate, a hydrophobic probe.
Journal ArticleDOI
Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates.
David C. Turner,Ludwig Brand +1 more
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Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalenesulfonate. Fluorimetric titrations.
Ezra Daniel,Gregorio Weber +1 more
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Nanosecond Time-Resolved Emission Spectroscopy: Spectral Shifts due to Solvent-Excited Solute Relaxation
TL;DR: In this article, it was demonstrated that the temperature-dependent spectral shifts are in fact due to time-dependent spectrum shifts, and at least two relaxation times characterize this phenomenon, one relaxation time is observed to be subnanosecond in character and may be associated with the exciplex that presumably is present in the system, while the other relaxation time was presumably associated with nonspecific dipolar reorientation although it has distinctly different characteristics from the solvent dielectric relaxation time.