title: Deuteration can affect the conformational behaviour of amphiphilic alpha-helical structures.
abstract: The replacement of hydrogen with deuterium is frequently used in conjunction with neutron diffraction to investigate peptide-membrane interaction. This isotopic substitution in an amino acid residue radically changes the neutron scatter pattern of the peptide, thereby allowing its localisation within the bilayer with the aid of derived Fourier maps. Nonetheless, this technique relies on the generally held assumption that normal and isotopically enriched protein species do not differ significantly in structure or biological activity. Recently, this assumption has been questioned and here, diffraction data from studies on a membrane interactive peptide clearly challenge the reliability of this assumption.
authors.affiliation: Faculty of Science, University of Central Lancashire, Preston, PR1 2HE, UK.
authors.forename: Sarah R
authors.initials: SR
authors.lastname: Dennison
authors.forename: Thomas
authors.initials: T
authors.lastname: Hauss
authors.forename: Silvia
authors.initials: S
authors.lastname: Dante
authors.forename: Klaus
authors.initials: K
authors.lastname: Brandenburg
authors.forename: Frederick
authors.initials: F
authors.lastname: Harris
authors.forename: David A
authors.initials: DA
authors.lastname: Phoenix
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003903:Deuterium; D008051:Lipid Bilayers / Q000737:chemistry; D033363:Neutron Diffraction / Q000379:methods; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012680:Sensitivity and Specificity; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods
chemical_list: D008051:Lipid Bilayers; D010455:Peptides; D003903:Deuterium