Literature DB >> 281678

Interacting enzyme systems at steady state: further Monte Carlo calculations on two-state molecules.

T L Hill, Y D Chen.   

Abstract

In this work, Monte Carlo calculations were made on a 10 x 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 x 10 lattice used in the exact calculations.

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Year:  1978        PMID: 281678      PMCID: PMC392940          DOI: 10.1073/pnas.75.11.5260

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  2 in total

1.  Theoretical study of the effect of enzyme-enzyme interactions on steady-state enzyme kinetics.

Authors:  T L Hill
Journal:  Proc Natl Acad Sci U S A       Date:  1977-09       Impact factor: 11.205

2.  Attitudes of women and men physicians.

Authors:  M Heins; J Hendricks; L Martindale; S Smock; M Stein; J Jacobs
Journal:  Am J Public Health       Date:  1979-11       Impact factor: 9.308

  2 in total
  4 in total

1.  Steady-state phase or cooperative transitions between biochemical cycles.

Authors:  T L Hill
Journal:  Proc Natl Acad Sci U S A       Date:  1979-02       Impact factor: 11.205

2.  Three-state, steady-state Ising systems: Monte Carlo and Bragg-Williams treatments.

Authors:  T L Hill; Y D Chen
Journal:  Proc Natl Acad Sci U S A       Date:  1981-01       Impact factor: 11.205

3.  Approximate steady-state properties of lattices of interacting three-state enzyme molecules: a novel phase transition.

Authors:  T L Hill; L Stein
Journal:  Proc Natl Acad Sci U S A       Date:  1979-03       Impact factor: 11.205

4.  Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin.

Authors:  T L Hill; E Eisenberg; J M Chalovich
Journal:  Biophys J       Date:  1981-07       Impact factor: 4.033

  4 in total

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