Unknown

Dataset Information

0

Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1.


ABSTRACT: Molecular docking and ANS-displacement experiments indicated that 8-anilinonaphthalene sulfonate (ANS) binds the hydrophobic site (H-site) in the active site of dimeric class Mu rGST M1-1. The naphthalene moiety provides most of the van der Waals contacts at the ANS-binding interface while the anilino group is able to sample different rotamers. The energetics of ANS binding were studied by isothermal titration calorimetry (ITC) over the temperature range of 5-30 degrees C. Binding is both enthalpically and entropically driven and displays a stoichiometry of one ANS molecule per subunit (or H-site). ANS binding is linked to the uptake of 0.5 protons at pH 6.5. Enthalpy of binding depends linearly upon temperature yielding a DeltaC(p) of -80+/-4 cal K(-1) mol(-1) indicating the burial of solvent-exposed nonpolar surface area upon ANS-protein complex formation. While ion-pair interactions between the sulfonate moiety of ANS and protein cationic groups may be significant for other ANS-binding proteins, the binding of ANS to rGST M1-1 is primarily hydrophobic in origin. The binding properties are compared with those of other GSTs and ANS-binding proteins.

SUBMITTER: Kinsley N 

PROVIDER: S-EPMC2603631 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1.

Kinsley Nichole N   Sayed Yasien Y   Mosebi Salerwe S   Armstrong Richard N RN   Dirr Heini W HW  

Biophysical chemistry 20080805 2-3


Molecular docking and ANS-displacement experiments indicated that 8-anilinonaphthalene sulfonate (ANS) binds the hydrophobic site (H-site) in the active site of dimeric class Mu rGST M1-1. The naphthalene moiety provides most of the van der Waals contacts at the ANS-binding interface while the anilino group is able to sample different rotamers. The energetics of ANS binding were studied by isothermal titration calorimetry (ITC) over the temperature range of 5-30 degrees C. Binding is both enthal  ...[more]

Similar Datasets

| S-EPMC3262591 | biostudies-literature
| S-EPMC1138746 | biostudies-other
| S-EPMC1217852 | biostudies-other
| S-EPMC1223192 | biostudies-other
| S-EPMC2242538 | biostudies-other
| S-EPMC3776957 | biostudies-literature
| S-EPMC1138858 | biostudies-other
| S-EPMC6928345 | biostudies-literature
| S-EPMC3965517 | biostudies-literature
| S-EPMC1220659 | biostudies-other