Alexander Bepperling
Technische Universität München
14 Papers
102 Citations
Alexander Bepperling is an academic researcher from Technische Universität München. The author has contributed to research in topics: Biology & Chaperone (protein). The author has an hindex of 9, co-authored 10 publications. Previous affiliations of Alexander Bepperling include Center for Integrated Protein Science Munich.
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Papers
Independent evolution of the core domain and its flanking sequences in small heat shock proteins
Thomas Kriehuber,Thomas Rattei,Thomas Weinmaier,Alexander Bepperling,Martin Haslbeck,Johannes Buchner +5 more
TL;DR: In this paper, the evolutionary history of small heat shock proteins (sHsps) is studied and two exon boundary-independent strategies are combined: the evolution of the conserved α-crystallin domain and the independent evolution of N- and C-terminal sequences.
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Alternative bacterial two-component small heat shock protein systems
Alexander Bepperling,Ferdinand Alte,Thomas Kriehuber,Nathalie Braun,Sevil Weinkauf,Michael Groll,Martin Haslbeck,Johannes Buchner +7 more
TL;DR: It is shown that these two sHsps are strikingly different in their quaternary structures and chaperone properties, defining a second type of bacterial two-component sHsp system.
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Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin.
Bin Huang,Tanja Lucas,Claudia Kueppers,Xiaomin Dong,Maike Krause,Alexander Bepperling,Johannes Buchner,Hans Voshol,Andreas Weiss,Bertran Gerrits,Stefan Kochanek +10 more
TL;DR: Differences in secondary structure between normal and mutant Htt, a helix-rich protein, were not observed in this study and Purified Htt tends to form dimers and higher order oligomers, thus resembling the situation observed with N-terminal fragments, although the mechanism of oligomer formation may be different.
Regions Outside the α-Crystallin Domain of the Small Heat Shock Protein Hsp26 Are Required for Its Dimerization
TL;DR: A thermodynamic analysis of the monomeric and dimeric constructs revealed that dimers are not significantly stabilized against thermal and chemical denaturation in comparison to monomers, supporting the notion that dimerization is not a prerequisite for the formation of a well-folded Hsp26 alpha-crystallin domain.
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Structural and functional diversity in the family of small heat shock proteins from the parasite Toxoplasma gondii
Natalia de Miguel,Nathalie Braun,Alexander Bepperling,Thomas Kriehuber,Andreas Kastenmüller,Johannes Buchner,Sergio O. Angel,Martin Haslbeck +7 more
TL;DR: This first in vitro characterization of small heat shock proteins from protists showed that all T. gondii sHsps exhibit the characteristic properties of sHSps such as oligomeric structure and chaperone activity, suggesting an adaption to specific steps of the parasite's life cycle.
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