Searching for Hydrodynamic Orienting Effects in the Association of Tri-N-acetylglucosamine with Hen Egg-White Lysozyme.

ABSTRACT: Using stopped-flow fluorometry, we determined rate constants for the formation of diffusional encounter complexes of tri-N-acetylglucosamine (NAG₃) with hen egg-white lysozyme (k_a^WT) and its double mutant Asp48Asn/Lys116Gln (k_a^MT). We defined binding anisotropy, κ ≡ (k_a^WT - k_a^MT)/(k_a^WT + k_a^MT), and determined its ionic strength dependence. Our goal was to check if this ionic strength dependence provides information about the orienting hydrodynamic effects in the ligand-binding process. We also computed ionic strength dependence of the binding anisotropy from Brownian dynamics simulations using simple

SUBMITTER: Wielgus-Kutrowska B 

PROVIDER: S-EPMC8488934 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature