Deuteration can affect the conformational behaviour of amphiphilic alpha-helical structures.
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.
Dennison
Sarah R
SR
Faculty of Science, University of Central Lancashire, Preston, PR1 2HE, UK.
Hauss
Thomas
T
Dante
Silvia
S
Brandenburg
Klaus
K
Harris
Frederick
F
Phoenix
David A
DA
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
D008051:Lipid Bilayers; D010455:Peptides; D003903:Deuterium