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The Amphiphilicity of ACP Helices: A Means of Macromolecular Interaction?

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.

Identiferoai:union.ndltd.org:ETSU/oai:dc.etsu.edu:etsu-works-12995
Date11 May 1987
CreatorsErnst-Fonberg, Mary L., Tucker, Margie Mc, Fonberg, Ignacy B.
PublisherDigital Commons @ East Tennessee State University
Source SetsEast Tennessee State University
Detected LanguageEnglish
Typetext
SourceETSU Faculty Works

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