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Interacting Enzyme Systems at Steady State: Further Monte Carlo Calculations on Two-State Molecules
Terrell L. Hill and Yi-Der Chen
Proceedings of the National Academy of Sciences of the United States of America
Vol. 75, No. 11 (Nov., 1978), pp. 5260-5263
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/68607
Page Count: 4
You can always find the topics here!Topics: Molecules, Approximation, Enzymes, Molecular interactions, Free energy
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In this work, Monte Carlo calculations were made on a 10 × 10 lattice of two-state, steady-state enzyme molecules in two special cases for which the Bragg-Williams (mean field) approximation had earlier produced some very interesting phase-transition properties. The Monte Carlo results proved to be similar to Bragg-Williams in some respects but not in others. The discrepancies are attributed primarily to: (i) inadequate treatment by Bragg-Williams of strong negative cooperativity; and (ii) the finite size of the 10 × 10 lattice used in the exact calculations.
Proceedings of the National Academy of Sciences of the United States of America © 1978 National Academy of Sciences