1984•BiopolymersRequires access

Quantitative aspects of the development of a hydrophobic binding site on calmodulin by calcium binding

Robert Frank Steiner

Abstract

Abstract The interactive binding by calmodulin of Ca2+ and 1‐anilinonaphthalene‐8‐sulfonate (1,8‐ANS) has been examined. In the presence of saturating levels of Ca2+, calmodulin develops one moderately strong binding site for 1,8‐ANS, plus one or more weaker sites. The binding of 1,8‐ANS by unliganded, or singly liganded, calmodulin is slight; the development of a strong binding site, as well as the characteristic fluorescence enhancement and CD spectrum, requires the binding of two Ca2+ ions. Little further change occurs on binding additional Ca2+ ions.

About this research paper

What this paper is about

Why it matters

OpenAlex reports 4 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Key concepts: Calmodulin, Chemistry, Binding site, Calcium, Calcium-binding protein, Fluorescence, Biophysics, Binding protein