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The amphiphilicity of ACP helices: A means of macromolecular interaction?
Author(s) -
Ernst-Fonberg Mary Lou,
Tucker Margie McGee,
Fonberg Ignacy B.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80158-8
Subject(s) - amphiphile , chemistry , helix (gastropod) , macromolecule , crystallography , hydrophobic effect , biophysics , biochemistry , biology , organic chemistry , polymer , ecology , snail , copolymer
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.