6-[Fluorescein-5(6)-carboxamido]hexanoic acid is used as a fluorescein-based fluorescent label for proteins that can be analyzed in applications such as quenching experiments.
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Biochimica et biophysica acta. General subjects, 1864(7), 129606-129606 (2020-04-02)
The comprehension of the mechanism of action of antimicrobial peptides is fundamental for the design of new antibiotics. Studies performed looking at the interaction of peptides with bacterial cells offer a faithful picture of what really happens in nature. In
Immune complexes were formed between dinitrophenylated human serum albumin (DNP-HSA) and polyclonal rabbit immunoglobulin G (IgG) anti-DNP antibodies at antibody excess. The antigen was labelled with isotope (125I-tyramine-cellobiose) or fluorochrome, (6-[fluorescein-5-(and-6)-carboxamido] hexanoic-acid, succinimidyl ester). The radiolabelled antigen, native or antibody
Production and properties of skeletal myosin subfragment 1 selectively labeled with fluorescein at lysine-553 proximal to the strong actin-binding site.
Archives of biochemistry and biophysics, 505(1), 105-111 (2010-10-05)
2,4-Dinitrophenol (DNP) increases the affinity of myosin for actin and accelerates its Mg(2+)ATPase activity, suggesting that it acts on a region of the myosin head that transmits conformational changes to actin- and ATP-binding sites. The binding site/s for DNP are
Lys-553 of skeletal muscle myosin subfragment 1 (S1) was specifically labeled with the fluorescent probe FHS (6-[fluorescein-5(and 6)-carboxamido]hexanoic acid succinimidyl ester) and fluorescence quenching experiments were carried out to determine the accessibility of this probe at Lys-553 in both the
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