Electrostatic controlled kinetics efficiency

Triose Phosphate Isomerase Diffusional Encounters with D-Glyceraldehyde-3-Phosphate In this section we use a real system, triose phosphate isomerase (TIM) and its substrate D-glyceraldehyde—3-phosphate (GAP) to demonstrate the capabilities of Brownian dynamics simulations with electrostatics. TIM is a glycolytic enzyme that catalyzes the interconversion of GAP and dihydroxy-acetone phosphate (DHAP). It has been described as an almost perfea catalyst because of its remarkable efficiency. Structurally, TIM is a dimeric enzyme consisting of two identical polypeptide chains of 247 amino acid residues. Each subunit consists of eight loop-p/loop-a units and contains one aaive site. Located near each aaive site is a peptide loop, which is mobile in the native enzyme and folds down to cover the active site when the substrate is bound. Kinetically, the reaction appears to be diffusion controlled and proceeds with a measured rate constant of 4.8 x 10 M s L TIM has consequently been the focus of many kinetic and struaural studies. ... 

The adsorption process of PLL-g-PEG on mica is controlled by electrostatic forces. Van do- Waals attraction, and stoic contributions that originate from the grafted PEG side chains. PEG2000 itself is of too low a molecular weight to adsorb efficiently on mica. The adsorption kinetics of... 

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