Christian Betzel
University of Hamburg
349 Papers
2.8K Citations
Christian Betzel is an academic researcher from University of Hamburg. The author has contributed to research in topics: Protein crystallization & Chemistry. The author has an hindex of 44, co-authored 330 publications. Previous affiliations of Christian Betzel include Eppendorf (Germany) & University of Tübingen.
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Papers
Mercury induced modifications in the stereochemistry of the active site through Cys-73 in a serine protease--crystal structure of the complex of a partially modified proteinase K with mercury at 1.8 A resolution.
Samudrala Gourinath,M. Degenhardt,Susanne Eschenburg,Karen M. Moore,Lawrence J. DeLucas,Christian Betzel,Tejbal Singh +6 more
TL;DR: Proteinese K (PK) isolated from Tritirachium album Limber was crystallized with HgCl2 in excess, under microgravity conditions and the binding of mercury distorts the stereochemistry of the neighbouring residues including those belonging to the catalytic triad.
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Two variants of the major serine protease inhibitor from the sea anemone Stichodactyla helianthus, expressed in Pichia pastoris.
Rossana García-Fernández,Patrick Ziegelmüller,Lidice González,Manuel Mansur,Yoan Machado,Lars Redecke,Ulrich Hahn,Christian Betzel,María A. Chávez +8 more
TL;DR: Two new ShPI-1 variants with modified inhibitory activities are provided, one of them with increased biomedical potential and new insight into the functional impact of the P1 and P2' sites on Sh PI-1 specificity are offered.
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Flip-Flop-Wasserstoffbrückenbindungen in β-Cyclodextrin - ein allgemein gültiges Prinzip in Polysacchariden?
TL;DR: Das vollstandige Manuskript dieser Zuschrift as mentioned in this paper was published in 1983, 1191, and it is available in Amazon.com for a limited time.
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Interactions of recombinant prions with compounds of therapeutical significance.
Dessislava Georgieva,Daniel Schwark,Martin von Bergen,Lars Redecke,Nicolay Genov,Christian Betzel +5 more
TL;DR: It is shown that the prion aggregates formed in the presence of six compounds have no beta-structure, which is typical of the infectious form, and possess considerably higher alpha-helical content than the normal PrP(C).
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The mistletoe lectin I--phloretamide structure reveals a new function of plant lectins.
Arne Meyer,Wojciech Rypniewski,Lech Celewicz,Volker A. Erdmann,Wolfgang Voelter,Tej P. Singh,Nicolay Genov,J. Barciszewski,Christian Betzel +8 more
TL;DR: The specific binding of PA to ML-I indicates that heterodimeric RIPs are multifunctional proteins whose functions in the cell have not yet been fully recognized and analyzed.
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