Applied Surface Science, Vol.235, No.1-2, 188-196, 2004
Tapping mode AFM study on the surface dynamics of a single glucose oxidase molecule on a Au(111) surface in water with implication for a surface-induced unfolding pathway
We have investigated a surface-induced unfolding dynamics of a single glucose oxidase (GO) molecule on Au(1 1 1) in air-saturated water, using tapping mode atomic force microscopy (TMAFM). We followed the unfolding process by measuring the maximum height of a well-isolated GO molecule on a terrace near a step-edge of the surface as a function of contact time. We find three linear portions with two intersections in a power-law fit to the selected values of the observed heights. The kinetic TMAFM result implies that there exist at least two distinct dynamic regimes in the unfolding. (C) 2004 Elsevier B.V. All rights reserved.
Keywords:tapping mode atomic force microscopy;A single protein molecule;surface-induced unfolding dynamics;unfolding pathway;glucose oxidase