title: Conformational behaviour of the TraM headpiece.
abstract: The structure of the headpiece of the TraM protein was investigated in different solvents. The very first 22 amino acids which alternate in their hydrophilic and hydrophobic character formed a helical structure in the presence of a membrane mimetic. In water alone the structure was flexible with a small amount of helicity according to circular dichroism measurements, whereas a loop structure was observed in dimethyl sulphoxide.
authors.affiliation: Institute of Organic Chemistry, Karl Franzens University Graz, Austria.
authors.forename: C
authors.initials: C
authors.lastname: Plugariu
authors.forename: T
authors.initials: T
authors.lastname: Stockner
authors.forename: D
authors.initials: D
authors.lastname: Moskau
authors.forename: G
authors.initials: G
authors.lastname: Koraimann
authors.forename: G
authors.initials: G
authors.lastname: Högenauer
authors.forename: H
authors.initials: H
authors.lastname: Sterk
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; C074281:TraM protein, bacterial