作者: Shigeki Mitaku , Satoru Hoshi , Ryoichi Kataoka
DOI: 10.1143/JPSJ.54.2047
关键词: Globular protein 、 Helix bundle 、 Alpha helix 、 Crystallography 、 Helix 、 Membrane protein 、 Chemistry 、 Peptide sequence 、 Hydrophobicity scales 、 Turn (biochemistry)
摘要: The average hydrophobicity as well the helix periodicity in amino acid sequence were compared among filamentous proteins, α-type globular proteins and intrinsic membrane order to study correlation between side chain arrangement environmental conditions around helices. Although content of those is equally high, power spectral density at period (3.6 residues per a turn) changed systematically three kinds revealing systematic distribution two types helical segments : hydrophobic amphiphilic analysis partial sequences showed that occurs interface polar nonpolar environment, while helixis found interior protein complex or membranes.