Three-dimensional lattice Monte Carlo simulations of model proteins. IV. Proteins at an oil-water interface.
Lattice Monte Carlo simulations describe the adsorption of protein-like heteropolymer chains at an oil/water interface. The heteropolymers are designed sequences of 27 and 64 amino acid-type lattice sites taken from a 20-letter alphabet. We use our recently suggested energy scale to model oil and water. We investigate the effect of the oil parameters on adsorption properties of a single chain and on the aggregation of adsorbed chains while keeping the water parameters fixed to their optimum values found previously. By varying the oil parameters, we can cause a large range of adsorption behavior: from no adsorption to reversible adsorption to irreversible adsorption. We compare adsorption at a liquid/solid interface to that at a liquid/liquid interface. A liquid interface leads to stronger adsorption and denaturation than a solid interface with the same water and oil interaction parameters. We propose "optimal" oil parameters and use them to study multichain adsorption at a liquid interface.
Leonhard
K
K
Lehrstuhl für Technische Thermodynamik, Schinkelstrasse 8, 52062 Aachen, Germany. leonhard@ltt.rwth-aachen.de
Prausnitz
J M
JM
Radke
C J
CJ
D000327:Adsorption; D008958:Models, Molecular; D009010:Monte Carlo Method; D009821:Oils / Q000737:chemistry*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D009821:Oils; D011506:Proteins; D014867:Water