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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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