title: The prediction of hydrophobicity gradients within membrane interactive protein alpha-helices using a novel graphical technique.
abstract: 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.
authors.affiliation: Department of Forensic and Investigative Sciences, University of Central Lancashire, Preston, PR1 2HE, UK.
authors.forename: Frederick
authors.initials: F
authors.lastname: Harris
authors.forename: Sarah
authors.initials: S
authors.lastname: Dennison
authors.forename: David A
authors.initials: DA
authors.lastname: Phoenix
mesh_terms: 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
chemical_list: D008565:Membrane Proteins