当前位置： SCI文献检索 > PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA期刊下所有文献 > Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex.

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

Abstract：

:Recent experimental data on the equilibrium binding of myosin subfragment 1 (S-1) to regulated actin filaments in the presence and in the absence of Ca(2+) are analyzed by using a linear Ising model. In the model, each tropomyosin-troponin unit (including seven sites on the actin filament) can be in one of two possible states, which have different intrinsic free energies and different binding constants for S-1. Bound S-1 molecules do not interact with each other. There are nearest-neighbor (pair) interactions between these units that depend on the state of each member of the pair and on the number of Ca(2+) bound to one member of the pair. There are two sources of positive cooperativity in this system: the fact that seven actin sites change state together as part of a single unit; and the existence of attractive nearest-neighbor interactions between units. Parameters in the model are evaluated by fitting the data, both in the presence and in the absence of Ca(2+). Several extensions of this model are discussed.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Hill TL,Eisenberg E,Greene L

doi

10.1073/pnas.77.6.3186

keywords:

subject

Has Abstract

pub_date

1980-06-01 00:00:00

pages

3186-90

issue

6

eissn

0027-8424

issn

1091-6490

journal_volume

77

pub_type

杂志文章

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