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 > Analytical and graphical examination of strong binding by half-of-sites in proteins: illustration with aspartate transcarbamylase.

Analytical and graphical examination of strong binding by half-of-sites in proteins: illustration with aspartate transcarbamylase.

Abstract：

:In multiple binding of ligands to a protein, the binding sites may seem to behave as if they are partitioned equally between two modalities. This paper analyzes three different molecular situations in which two actual assemblages appear: (i) two classes of sites exist at the outset in the ligand-free macromolecule; (ii) all sites are initially identical but after half are occupied, the affinity of the residual ones is altered; (iii) all sites are initially identical but they interact in a pairwise manner. The contours of affinity profiles-graphs of normalized stoichiometric binding constants (iK(i)) versus stoichiometric step number i-are examined for each situation to provide a basis for discriminating among them. Proper procedures for evaluating the site binding constants are then described. To illustrate these procedures, published experimental data for two real systems, binding of substrate or modifier by the enzyme aspartate transcarbamylase (carbamoylphosphate: L-aspartate carbamoyltransferase, EC 2.1.3.2), are scrutinized and the meaning of the calculated binding parameters is examined. The results demonstrate concretely that site binding constants cannot be specified without assuming a particular molecular model, but the stoichiometric constants can be assigned unambiguously without regard to the type of behavior at the individual sites.

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

Klotz IM,Hunston DL

doi

10.1073/pnas.74.11.4959

subject

Has Abstract

pub_date

1977-11-01 00:00:00

pages

4959-63

issue

11

eissn

0027-8424

issn

1091-6490

journal_volume

74

pub_type

杂志文章

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