title: Conformation and pairing properties of the N-terminal fragments of trichorzianine and alamethicin: a theoretical study.
abstract: Energy optimizations are carried out on the N-terminal fragment of trichorzianine in comparison to that of alamethicin. The results indicate that the helical character of the (Ac...Pro13) sequence of trichorzianine (TA IIIc) is essentially alpha with a bend in the helix axis in the end proline region, a structure comparable to the optimal alpha-helical structure of the corresponding segment (Ac...Pro14) of alamethicin AI. However, two weak n----n + 3 interactions coexist in trichorzianine with the alpha-helical n----n + 4 hydrogen bonds. The possible role of the glutamine side-chains in pairing such segments together is considered.
authors.affiliation: Institut de Biologie Physico-Chimique, C.N.R.S., Paris, France.
authors.forename: S
authors.initials: S
authors.lastname: Furois-Corbin
authors.forename: A
authors.initials: A
authors.lastname: Pullman
mesh_terms: D000408:Alamethicin; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D054848:Peptaibols; D010446:Peptide Fragments; D010455:Peptides; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D000900:Anti-Bacterial Agents; D054848:Peptaibols; D010446:Peptide Fragments; D010455:Peptides; D000408:Alamethicin; C039715:trichorzianine