Literature DB >> 16592620

Steady-state phase or cooperative transitions between biochemical cycles.

T L Hill1.   

Abstract

In a steady-state lattice of interacting enzyme molecules that have a multicycle kinetic diagram, a cooperative or phase transition may involve not only the conventional sudden change in the relative importance of the different states of a molecule but also a sudden change in the dominant cycles of the diagram. The latter effect implies a sudden switch in the dominant biochemistry (e.g., a sudden onset of active transport). An explicit example is discussed.

Year:  1979        PMID: 16592620      PMCID: PMC383027          DOI: 10.1073/pnas.76.2.714

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


  4 in total

1.  Interacting enzyme systems at steady state: location of the phase transition in approximations of the mean field type.

Authors:  T L Hill; Y D Chen
Journal:  Proc Natl Acad Sci U S A       Date:  1978-07       Impact factor: 11.205

2.  Further 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:  1977-10       Impact factor: 11.205

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

Authors:  T L Hill; Y D Chen
Journal:  Proc Natl Acad Sci U S A       Date:  1978-11       Impact factor: 11.205

4.  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

  4 in total
  4 in total

1.  Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex.

Authors:  T L Hill; E Eisenberg; L Greene
Journal:  Proc Natl Acad Sci U S A       Date:  1980-06       Impact factor: 11.205

2.  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

3.  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.  Subunit neighbor interactions in enzyme kinetics: half-of-the-sites reactivity in a dimer.

Authors:  T L Hill; A Levitzki
Journal:  Proc Natl Acad Sci U S A       Date:  1980-10       Impact factor: 11.205

  4 in total

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