1-Anilino-8-Naphthalene Sulfonate Anion-Protein Binding Depends Primarily on Ion Pair Formation
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چکیده
منابع مشابه
1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation.
The ANS- (1-anilino-8-naphthalene sulfonate) anion is strongly, dominantly bound to cationic groups of water-soluble proteins and polyamino acids through ion pair formation. This mode of ANS- binding, broad and pH dependent, is expressed by the quite rigorous stoichiometry of ANS- bound with respect to the available summed number of H+ titrated lysine, histidine, and arginine groups. By titrati...
متن کاملAn electrospray ionization mass spectrometry investigation of 1-anilino-8-naphthalene-sulfonate (ANS) binding to proteins.
The binding of 1-anilino-8-naphthalene-sulfonic acid (ANS) to various globular proteins at acidic pH has been investigated by electrospray ionization mass spectrometry (ESI-MS). Maximal ANS binding is observed in the pH range 3-5. As many as seven species of dye-bound complexes are detected for myoglobin. Similar studies were carried out with cytochrome c, carbonic anhydrase, triosephosphate is...
متن کامل8-Quinolyl 5-(dimethylamino)naphthalene-1-sulfonate
In the title compound, C(21)H(18)N(2)O(3)S, the dihedral angle between the naphthalene and quinoline ring systems is 55.53 (2)°, and the torsion angle involving the connecting C-S-O-C atoms is 87.60 (3)°. In the crystal structure, weak inter-molecular C-H⋯O hydrogen bonds connect mol-ecules into chains along [100] and there are π-π stacking inter-actions between pairs of chains with a centroid-...
متن کاملThe use of 1-anilino-8-naphthalene sulfonate as fluorescent probe for conformational studies on ribulose-1,5-bisphosphate carboxylase.
The influence of Mg2+ ions and temperature on the structure of the enzyme ribulose-1,5-bisphosphate carboxylase was investigated using the fluorescent probe 1-anilino-8-naphthalene sulfonate (ANS). The binding of ANS to the enzyme molecule caused a significant increase of fluorescence emission which was further enhanced by the addition of Mg2+. The temperature dependence of the fluorescence emi...
متن کامل1-Anilino-8-Naphthalene Sulfonate (ANS) Is Not a Desirable Probe for Determining the Molten Globule State of Chymopapain
The molten globule (MG) state of proteins is widely detected through binding with 1-anilino-8-naphthalene sulphonate (ANS), a fluorescent dye. This strategy is based upon the assumption that when in molten globule state, the exposed hydrophobic clusters of protein are readily bound by the nonpolar anilino-naphthalene moiety of ANS molecules which then produce brilliant fluorescence. In this wor...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1998
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(98)77799-9