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Journal ArticleDOI

Fluorescence quenching studies with proteins.

TLDR
A review of the use of the technique of solute fluorescence quenching to study the structure and dynamics of proteins and a number of factors are discussed that must be considered in analyzing such data.
About
This article is published in Analytical Biochemistry.The article was published on 1981-07-01. It has received 1644 citations till now. The article focuses on the topics: Quenching (fluorescence).

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Citations
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Journal ArticleDOI

Hydrogen exchange and structural dynamics of proteins and nucleic acids

TL;DR: Though the structures presented in crystallographic models of macromolecules appear to possess rock-like solidity, real proteins and nucleic acids are not particularly rigid.
Journal ArticleDOI

Tris(phenanthroline)ruthenium(II) enantiomer interactions with DNA: Mode and specificity of binding

TL;DR: The results of these studies indicated that both isomers bind to DNA by a single mode, but the two isomers differ, however, in their effect on the hydrodynamic properties of DNA as measured by viscosity and, therefore, probably differ in their individual binding modes.
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Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure.

TL;DR: It is indicated that low concentrations of some metals can directly induce alpha-synuclein fibril formation and the potential for ligand bridging by polyvalent metal ions is proposed to be an important factor in the metal-induced conformational changes of alpha- synuclein.
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Interaction of drugs with bovine and human serum albumin

TL;DR: Fluorescence emission spectra of serum albumin in the presence of MMI or PTU, recorded at the excitation wavelengths 280 and 295 nm, clearly show that the studied drugs act as quenchers.
References
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Journal ArticleDOI

Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules.

Joseph R. Lakowicz, +1 more
- 09 Oct 1973 - 
TL;DR: In this article, the fluorescence of various fluorophores by molecular oxygen has been studied in aqueous and nonaqueous solutions equilibrated with oxygen pressures up to 100 atm.
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Dynamics of folded proteins

TL;DR: The dynamics of a folded globular protein have been studied by solving the equations of motion for the atoms with an empirical potential energy function and suggest that the protein interior is fluid-like in that the local atom motions have a diffusional character.
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Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion.

Sherwin S. Lehrer
- 17 Aug 1971 - 
TL;DR: The results of the model compound study provide evidence for a mechanism that follows the classical Stern-Volmer law (1919), predominantly involving collisional quenching, and illustrate the importance of local charge and solvent viscosity.
Journal ArticleDOI

Dynamics of ligand binding to myoglobin

TL;DR: The nonexponential rebinding observed at low temperatures and in solid samples implies that the innermost barrier has a spectrum of activation energies, similar to how myoglobin achieves specificity and order.