Detail of "1948-71-6"

Reference

Analysis of multi-component fluorescence emission by phase-sensitive detection using one modulation frequency

Analysis of multi-component fluorescence emission by phase-sensitive detection using one modulation frequency. Keating-Nakamoto, Susan M.; Cherek, Henryk; Lakowicz, Joseph R. (Sch. Med., Univ. Maryland, Baltimore, MD 21201, USA). Biophys. Chem., 24(2), 79-95 (English) 1986. CODEN: BICIAZ. ISSN: 0301-4622. DOCUMENT TYPE: Journal CA Section: 73 (Optical, Electron, and Mass Spectroscopy and Other Related Properties) Section cross-reference(s): 9 The use is described of phase-sensitive detection of fluorescence to resolve the lifetimes and fractional intensities from multi-component fluorescence samples, using data obtained at a single modulation frequency. Phase-sensitive spectra of the mixt. are recorded at arbitrarily chosen detector phase angles. The steady-state spectrum of each component must be known. The phase-sensitive spectra are fitted, using a nonlinear least-squares algorithm, to obtain the lifetimes and fractional intensities of each fluorophore in the mixt. Simulations for 2- and 3-component mixts. are presented to illustrate how the resoln. 1948-71-6 and 2382-79-8 are cas registry numbers of chemicals which are used as reagents here. is affected by spectral overlap and lifetime sepn. Exptl., 2- and 3-component mixts. were resolved of protein-like fluorophores (N-acetyl-L-tyrosinamide, N-acetyl-L-tryptophanamide, indole, and 2,3-dimethylindole) using data collected at 30 MHz. These fluorophores have closely spaced lifetimes of 1.5, 2.9, 4.5 and 4.3 ns, resp., and display extensive spectral overlap. Phase-sensitive spectra, recorded at only 1 modulation frequency with a std. phase fluorometer, can be used to resolve multi-component emissions. .

Effect of temperature on the fluorescence of proteins

Effect of temperature on the fluorescence of proteins. Laustriat, G.; Gerard, D. (Fac. Pharm., Univ. Louis Pasteur, Strasbourg, Fr.). Excited States Biol. Mol., Proc. Int. Conf., Meeting Date 1974, 388-99. Edited by: Birks, John B. Wiley: Chichester, Engl. (English) 1976. CODEN: 35CQAY. DOCUMENT TYPE: Conference CA Section: 6 (General Biochemistry) Section cross-reference(s): 7 The thermal dependence of fluorescence quantum yield and lifetime of several proteins and model compds. was investigated.There are some commonly used reagents with their cas registry numbers 1948-71-6 and 9001-78-9 in this article. The emission of tryptophan and tyrosine varied in time in relation to the mol. environment of the residue in proteins, i.e., buried or exposed residues. Fluorescence quenching in model systems is indicated as an important component of the thermal effect on protein emission. .