Hilleria longifolia (H. Walter), n. sp.

Ohne Zusammenfassung     

Drei Höhe(n)punkte am Mittelrhein. Die Exkursion

Three highlights on the Middle Rhine The Upper Middle Rhine valley, part of the UNESCO World Heritage since 2002, has long been known as a classical travel region due to the impressive beauty of its landscape. The steep und narrow canyon comprises a complex series of remarkable geo‐ along with biotopes. These are characterized by their unique tectonics as well as by their floristic and faunistic elements. This excursion proposal highlights three selected destinations on the borderline of the valley which particularly appear equally promising and recommendable.     

Further Studies on the Genus Hypoblepharina Böhmig (Turbellaria, Dalyellioida), with Description of H. serrifera sp. n.

H. serrifera is described and supplementary information given on H. boehmigi . The material of both species was collected from the brood pouch of amphipods, H. serrifera from Orchomene no-dimanus (Walker). The studies complete our general picture of the anatomy of the genus Hypoblepharina and support the theory that all the species of this genus are commensals in amphipods.     

Malalcahuello ocaresi gen. & sp. n. (Elateridae,Campyloxeninae)

Malalcahuello ocaresi gen. n. & sp. n., from Chile, is described and compared with Campyloxenus pyrothorax Fairmaire & Germain, 1860.     

Isolation and structural analyses of positional isomers of 6(1),6(n)-di-O-(N-acetyl-beta-D-glucosaminyl)cyclomaltoheptaose (n=2, 3, and 4) and 6-O-[6-O-(N-acetyl-beta-D-glucosaminyl)-N-acetyl-beta-D-glucosaminyl]cyclomaltoheptaose.

6-O-[6-O-(N-acetyl-beta-D-glucosaminyl)-N-acetyl-beta-D-glucosaminyl]cyclomaltoheptaose (beta CD) and three positional isomers of 6(1),6(n)-di-O-(N-acetyl-beta-D-glucosaminyl)cyclomaltoheptaose (n=2, 3, and 4) in a mixture of products from beta CD and N-acetylglucosamine by the reversed reaction of beta-N-acetylhexosaminidase from jack bean were isolated and purified by HPLC. The structures of four isomers of di-N-acetylglucosaminyl-beta CDs were determined by FABMS and NMR spectroscopy. The degree of polymerization of the branched oligosaccharides produced by enzymatic degradation with bacterial saccharifying alpha-amylase (BSA) was established by LC-MS methods.     

Basipodella harpacticola n.gen., n. sp. (Crustacea,Copepoda)

Several stages of the copepodBasipodella harpacticola n. gen., n. sp., which lives as a parasite on harpacticoid copepods, are described on the basis of four individuals obtained from the Peruvian deep-sea. The taxonomic position of the new species is discussed.     

Melampyrum Moravicum H. Braun. n. sp.

Ohne Zusammenfassung     

Tylenchocriconema alleni n. g., n. sp. from Guatemala (Tylenchocriconematidae n. fam.; Tylenchocriconematidae n. superfam.; Nematoda)

Tylenchocriconema alleni n.g.n.sp, is described from soil about roots of a bromeliad from Guatemala City, Guatemala. It has characteristics of both the Tylenchoidea and Criconematoidea. Tylenchocriconematidae, n. fam., and Tylenchocriconematoidea, n. superfam., are proposed to express the relationship of this species to other taxa. Tylenchulidae and Paratylenchidae are considered closely related, and Tylenchulidoidea, n. rank, is proposed to indicate their relationship.     

Conformations of Gly(n)H+ and Ala(n)H+ peptides in the gas phase

High-resolution ion mobility measurements and molecular dynamics simulations have been used to probe the conformations of protonated polyglycine and polyalanine (Gly(n)H and Ala(n)H+, n = 3-20) in the gas phase. The measured collision integrals for both the polyglycine and the polyalanine peptides are consistent with a self-solvated globule conformation, where the peptide chain wraps around and solvates the charge located on the terminal amine. The conformations of the small peptides are governed entirely by self-solvation, whereas the larger ones have additional backbone hydrogen bonds. Helical conformations, which are stable for neutral Alan peptides, were not observed in the experiments. Molecular dynamics simulations for Ala(n)H+ peptides suggest that the charge destabilizes the helix, although several of the low energy conformations found in the simulations for the larger Ala(n)H+ peptides have small helical regions.