Franziska Thomas
University of Göttingen
18 Papers
47 Citations
Franziska Thomas is an academic researcher from University of Göttingen. The author has contributed to research in topics: Chemistry & Peptide. The author has an hindex of 9, co-authored 18 publications. Previous affiliations of Franziska Thomas include Heidelberg University & University of Bristol.
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Papers
Modular Design of Self-Assembling Peptide-Based Nanotubes
Natasha C. Burgess,Thomas H. Sharp,Franziska Thomas,Christopher W. Wood,Andrew R. Thomson,Nathan R. Zaccai,R. Leo Brady,Louise C. Serpell,Derek N. Woolfson +8 more
TL;DR: It is shown that blunt-ended α-helical barrels, that is, preassembled bundles of α-helices with central channels, can be used as building blocks for PNTs, which reveal that the overall symmetry of the peptide module plays a critical role in ripening and ordering of the supramolecular assembly.
Carbon Nanotubes Encapsulated in Coiled‐Coil Peptide Barrels
Florian A. Mann,Jan Horlebein,Nils Frederik Meyer,Daniel Meyer,Franziska Thomas,Sebastian Kruss +5 more
TL;DR: This approach presents a novel concept to encapsulate, discriminate and functionalize SWCNTs non-covalently with peptides and holds great promise for future applications in bioimaging or drug delivery.
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Conformational dynamics of asparagine at coiled-coil interfaces
TL;DR: This work probes the structure and dynamics of a de novo-designed coiled-coil homodimer, CC-Di, by multidimensional nuclear magnetic resonance spectroscopy, including model-free dynamical analysis and relaxation–dispersion experiments, and finds dynamic exchange on the millisecond time scale between Asn conformers with the side chains pointing into and out of the core.
Accessibility, Reactivity, and Selectivity of Side Chains within a Channel of de Novo Peptide Assembly
Antony J. Burton,Franziska Thomas,Christopher R. Agnew,Kieran L. Hudson,Stephen E. Halford,R. Leo Brady,Derek N. Woolfson +6 more
TL;DR: It is shown that multiple thiol moieties can be placed within a central channel of a de novo, six-helix peptide assembly (CC-Hex), and that it is possible to engineer reactive side chains with both precision and control into aDe novo scaffold to produce protein-like structures with chemoselective reactivity.
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Kinetic studies on strand displacement in de novo designed parallel heterodimeric coiled coils.
TL;DR: Strand displacement in heterodimeric coiled coils follows a competitive binding mechanism and can be predicted by the ratio of KD values.