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Title: Kinetics and Thermodynamics of 1-anilino-8-naphthalene Sulfonate Interactions with Urinary Trypsin Inhibitor.
Authors: Zuo, Zhenyu; Fan, Handong; Guo, Jianjun; Zhou, Wei; Li, Lingling
Abstract: The interactions between Urinary Trypsin Inhibitor (UTI) and 1-anilino-8-naphthalene sulfonate (ANS) were investigated by fluorescence spectra, isothermal titration calorimetry and molecular modeling. The results revealed the presence of four specific binding sites for ANS on UTI, with interactions driven mainly by electrostatic forces. The four specific binding sites indicated the involvement of four hydrophobic patches on UTI. Experimental data also confirmed the presence of a further five nonspecific binding sites that interacted mainly by the formation of salt bridges between the sulfonates of ANS and positive residues on the surface of UTI.
Subjects: THERMODYNAMICS; URINARY trypsin inhibitor; NAPHTHALENE; SULFONATES; CHEMICAL kinetics; PROTEIN-protein interactions; FLUORESCENCE spectroscopy; ISOTHERMAL titration calorimetry
Publication: Protein Journal, 2012, Vol 31, Issue 7, p585
ISSN: 1572-3887
Publication type: Academic Journal
DOI: 10.1007/s10930-012-9443-4

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Kinetics and Thermodynamics of 1-anilino-8-naphthalene Sulfonate Interactions with Urinary Trypsin Inhibitor.