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.
D000213:Acyl Carrier Protein; D000818:Animals; D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004926:Escherichia coli; D009124:Muscle Proteins; D010940:Plant Proteins; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D009124:Muscle Proteins; D010940:Plant Proteins