Work

The amphiphilicity of ACP helices: A means of macromolecular interaction?

Year: 1987

Type: article

Abstract: ACP interacts with diverse proteins in an unknown way. Possibly there is a similar mode of interaction between ACP and all ACP-binding proteins, the amphiphilic helix. The hydrophobicities of helices from 4 different ACPs were compared. Hydrophobic moment plots were prepared for ACP helices and those of many EF hand calcium-binding proteins. Both groups of proteins occupied the same region of the plot.

Source: FEBS Letters

DOI: 10.1016/0014-5793(87)80158-8

Authors: Mary Lou Ernst-Fonberg, Margie McGee Tucker, Ignacy B. Fonberg

Institution: East Tennessee State University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: National Science Foundation

Award: Enzymology of Lipid Biosynthetic Systems