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Monte Carlo simulation of the kinetics of protein adsorption
Author(s) -
Zhdanov V.P.,
Kasemo B.
Publication year - 1998
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19980201)30:2<177::aid-prot7>3.0.co;2-k
Subject(s) - denaturation (fissile materials) , kinetics , metastability , thermodynamics , adsorption , reaction rate constant , chemistry , diffusion , monte carlo method , constant (computer programming) , kinetic monte carlo , kinetic energy , chemical physics , physics , mathematics , organic chemistry , statistics , quantum mechanics , computer science , nuclear chemistry , programming language
Adsorption of proteins occurs via diffusion toward the interface, actual adsorption, and subsequent irreversible conformational changes resulting in denaturation of the native protein structure. The conventional kinetic models describing these steps are based on the assumption that the denaturation transitions obey the first‐order law with a single value of the denaturation rate constant k r . Meanwhile, recent Monte Carlo simulations indicate that, in general, the denaturation process cannot be described by a single rate constant k r . One should rather introduce a distribution of this rate constant (physically, different values of k r correspond to the transitions to the altered state via different metastable states). We have calculated the kinetics of irreversible adsorption of proteins with and without distribution of the denaturation rate constant k r in the limits when protein diffusion in the solution is, respectively, rapid or slow. In both cases, the adsorption kinetics with distribution of k r are found to be close to those with a single‐valued rate constant k r provided that the average value of k r in the former case is equal to k r for the latter case. This conclusion holds even for wide distributions of k r . The consequences of this finding for the fitting of global experimental kinetics on the basis of phenomenological equations are briefly discussed. Proteins 30:177–182, 1998. © 1998 Wiley‐Liss, Inc.