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“…Tryptophan appears to be the most favorable amino acid for charge-transfer interactions based on the theoretical calculations of Pullman and Pullman (1958). The observations in this study are in agreement with several studies of antibody-ligand complexation involving tryptohan residues in the antibody binding site (Jackson and Dwek, 1981;Templeton and Ware, 1985).…”
Section: Discussionsupporting
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“…Tryptophan appears to be the most favorable amino acid for charge-transfer interactions based on the theoretical calculations of Pullman and Pullman (1958). The observations in this study are in agreement with several studies of antibody-ligand complexation involving tryptohan residues in the antibody binding site (Jackson and Dwek, 1981;Templeton and Ware, 1985).…”
Section: Discussionsupporting
“…Their prediction gained support from several experimental observations (Isenberg and Szent-Gyorgi, 1958;Fujimori, 1959;Harbury et al, 1959;Cilento and Tedeschi, 1961;Foster and Hanson, 1965;Silifkin and Heathcote, 1968). Charge-transfer interaction between fluorescein and tryptophan in antibody-ligand complexes has been observed (Templeton and Ware, 1985). The importance of tryptophan in antibody binding to dinitrophenol has been well documented (Jackson and Dwek, 1981).…”
Section: Introductionmentioning
“…Two different groups (Watt and Voss, 1977;Templeton and Ware, 1985) have investigated the quenching mechanism and concluded that it involves formation of a charge transfer complex between fluorescein, in the excited state, and a neighboring tryptophan residue. This mechanism is consistent with the tbreedimensional structure of the antigen-binding fragment of an antifluorescein antibody in complex with fluorescein (Herron et al, 1989.…”
Section: 32b Fluorescence Quenchingmentioning
“…When the peptides bound to the labeled targets, the Xuorescence of AF was quenched, possibly because of interactions between the Xuorophore and the tryptophan residues in the peptides, although other mechanisms (Xuorescent resonance energy transfer, change in microenvironment, etc.) might also have been involved [13,[34][35][36]. The Xuorescent dyes were covalently attached via a succinimidyl ester bond to primary amines in the target proteins.…”
Section: Covalent Labeling Of Target Moleculesmentioning
“…FQ may also be used to measure changes in Xuorescent output of dyes that are covalently cross-linked to a target molecule (extrinsic Xuorophores) and are excited by wavelengths in the visible spectrum. Binding of the ligand to the labeled target induces conformational and/or energy changes, which alter the microenvironment of the extrinsic or intrinsic Xuorophore [12,13]. This causes a change (quenching or enhancement) in emission intensity.…”
mentioning