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Matthias Liebergesell

Researcher at University of Göttingen

Publications -  17
Citations -  1448

Matthias Liebergesell is an academic researcher from University of Göttingen. The author has contributed to research in topics: Peptide sequence & PHA granule. The author has an hindex of 14, co-authored 17 publications receiving 1421 citations. Previous affiliations of Matthias Liebergesell include Metabolix & University of Münster.

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Molecular basis for biosynthesis and accumulation of polyhydroxyalkanoic acids in bacteria

TL;DR: Molecular data will be shown for genes of Alcaligenes eutrophus, purple non-sulfur bacteria, Such as Rhodospirillum rubrum, purple sulfur bacteria, such as Chromatium vinosum, pseudomonads belonging to rRNA homology group I, and for the Gram-positive bacterium Rhodococcus ruber.
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Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acid inclusions

TL;DR: Some mathematical calculations were done that provided information about the structure and biochemistry of polyhydroxyalkanoic acid (PHA) granules and about the amounts of the different constituents that contribute to the PHA granules.
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Formation of poly(3-hydroxyalkanoates) by phototrophic and chemolithotrophic bacteria

TL;DR: Among 15 strains tested, only Chromatium vinosum strain 1611, C. purpuratum strain BN5500 and Lamprocystis roseopersicina strain 3112 were able to synthesize polyesters containing 3HV with propionate, valerate or heptanoate as carbon source.
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Cloning and nucleotide sequences of genes relevant for biosynthesis of poly(3-hydroxybutyric acid) in Chromatium vinosum strain D

TL;DR: From a genomic library of Chromatium vinosum strain D in lambda L47, a 16.5-kbp EcoRI-restriction fragment was identified by hybridization with a DNA fragment harboring the operon for Alcaligenes eutrophus poly(3-hydroxyalkanoate) (PHA) synthesis, which restored the ability to synthesize and accumulate PHA in PHA-negative mutants of A. eUTrophus.
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Purification and characterization of the poly(hydroxyalkanoic acid) synthase from Chromatium vinosum and localization of the enzyme at the surface of poly(hydroxyalkanoic acid) granules.

TL;DR: Immunoblots with anti-PhaC, anti- PhaE IgG and crude extract proteins indicated that poly(3-hydroxyalkanoic acid) synthases with partial sequence similarities are widespread among purple sulphur bacteria.