The conserved disulfide bond of human tear lipocalin modulates conformation and lipid binding in a ligand selective manner

Article ID	Journal	Published Year	Pages	File Type
10537388	Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics	2011	13 Pages	PDF

Abstract

âº Disulfide reduction promotes the plasticity for the hairpin CD. âº The time constant of binding kinetics for NBD cholesterol is decreased 3 fold. âº However, the time constant of binding kinetics for NBD C12-HPC is only slightly decreased. âº Disulfide reduction promotes conformational changes to favor binding the bulky ligand.

Keywords

NATA N-acetyl-L-tryptophanamide DAUDA 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid 1,5-IAEDANS Fluorescence resonance energy transfer FRET Tris(2-carboxyethyl) phosphine hydrochloride circular dichroism TCEP Time-resolved fluorescence Tear lipocalin Lipocalin-1 Ligand binding Protein dynamic