title: The conformation of cyclo(-D-Pro-Ala4-) as a model for cyclic pentapeptides of the DL4 type.
abstract: The conformation of the cyclic pentapeptide cyclo(-D-Pro-Ala(4)-) in solution and in the solid state was reinvestigated using modern NMR techniques. To allow unequivocal characterization of hydrogen bonds, relaxation behavior, and intramolecular distances, differently labeled isotopomers were synthesized. The NMR results, supported by extensive MD simulations, demonstrate unambiguously that the preferred conformation previously described by us, but recently questioned, is indeed correct. The validation of the conformational preferences of this cyclic peptide is important given that this system is a template for several bioactive compounds and for controlled "spatial screening" for the search of bioactive conformations.
authors.affiliation: Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.
authors.forename: Markus
authors.initials: M
authors.lastname: Heller
authors.forename: Martin
authors.initials: M
authors.lastname: Sukopp
authors.forename: Natia
authors.initials: N
authors.lastname: Tsomaia
authors.forename: Michael
authors.initials: M
authors.lastname: John
authors.forename: Dale F
authors.initials: DF
authors.lastname: Mierke
authors.forename: Bernd
authors.initials: B
authors.lastname: Reif
authors.forename: Horst
authors.initials: H
authors.lastname: Kessler
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives*; D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D006860:Hydrogen Bonding; D007553:Isotope Labeling; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry*; D011392:Proline / Q000031:analogs & derivatives*; D011487:Protein Conformation; D012996:Solutions / Q000737:chemistry; D013997:Time Factors
chemical_list: D010456:Peptides, Cyclic; D012996:Solutions; D011392:Proline; D000409:Alanine