The prediction of hydrophobicity gradients within membrane interactive protein alpha-helices using a novel graphical technique.
Here, it is shown that amphiphilicity profiling based on the mean hydrophobic moment provides a simple visual guide for the identification of oblique orientated alpha-helices. The methodology has an efficiency of circa 70% and predicts that approximately 40% of transmembrane alpha-helices may possess these structures.
Harris
Frederick
F
Department of Forensic and Investigative Sciences, University of Central Lancashire, Preston, PR1 2HE, UK.
Dennison
Sarah
S
Phoenix
David A
DA
D000465:Algorithms; D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism*; D019295:Computational Biology / Q000379:methods*; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary
D008565:Membrane Proteins