Correction: Thioamide quenching of intrinsic protein fluorescence
نویسندگان
چکیده
منابع مشابه
Thioamide quenching of intrinsic protein fluorescence.
Thioamides quench tryptophan and tyrosine fluorescence in a distance-dependent manner and thus can be used to monitor the binding of thioamide-containing peptides to proteins. Since thioamide analogs of the natural amino acids can be synthetically incorporated into peptides, they can function as minimally-perturbing probes of protein/peptide interactions.
متن کاملFluorescence Quenching of Green Fluorescent Protein during Denaturation by Guanidine
Fluorescence of green fluorescent protein mutant, 2-5 GFP is observed during denaturation by guanidine. The fluorescence intensity decreases exponentially but the fluorescence lifetime does not change during denaturation. The fluorescence lifetime of the denatured protein is shorter than that of native form. As the protein structure is modified by guanidine, solvent water molecules penetrate in...
متن کاملMCR of the quenching of the EEM of fluorescence of Aflatoxins (B1, G1) by Gold nanoparticles
In This research, gold nanoparticles were synthesized and functionalized by the antibody of aflatoxins. The quenching of the fluorescence of excitation emission matrices (EEM) of two type of aflatoxins (B1, G1), provoked by the gold nanoparticles, was studied by principal component analysis (PCA) and multivariate curve resolution with alternating least squares (MCR-ALS). These aflatoxins show q...
متن کاملLaboratory Exercises Protein Tryptophan Accessibility Studied by Fluorescence Quenching
A laboratory class is described to introduce the biochemistry major students to the basic concepts and various applications of fluorescence spectroscopy. Through simple and inexpensive experiments the students learn how to record excitation and emission spectra and measure intrinsic protein fluorescence and its quenching to elucidate the local tryptophan environment. Free tryptophan, ovalbumin,...
متن کاملQuenching of intrinsic fluorescence of sperm specific LDH by optical isomers of gossypol.
Intrinsic fluorescence of LDH-C4 has been studied in the presence of optical isomers of gossypol. The study showed that fluorescence due to tryptophan residues after excitation of LDH at 282 nm is quenched by each gossypol enantiomere in a concentration dependent manner. Half of the maximum quench (Q50%) of enzyme occurred with gossypol (-) at 0.9 x 10(-4) mol/l and with gossypol (+) at 1.4 x 1...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Chemical Communications
سال: 2020
ISSN: 1359-7345,1364-548X
DOI: 10.1039/d0cc90120b