T
Thomas Raschle
Researcher at Harvard University
Publications - 24
Citations - 2012
Thomas Raschle is an academic researcher from Harvard University. The author has contributed to research in topics: Membrane protein & ATP synthase. The author has an hindex of 19, co-authored 24 publications receiving 1869 citations. Previous affiliations of Thomas Raschle include University of Basel & ETH Zurich.
Papers
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Journal ArticleDOI
Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins
TL;DR: This paper demonstrates that the combination of small nanodisc size, high deuteration levels of protein and lipids, and the use of advanced non-uniform NMR sampling methods enable the NMR resonance assignment as well as the high-resolution structure determination of polytopic membrane proteins in a detergent-free, near-native lipid bilayer setting.
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Vitamin B6 biosynthesis in higher plants
Marina Tambasco-Studart,Olca Titiz,Thomas Raschle,Gabriela Forster,Nikolaus Amrhein,Thérésa Bridget Fitzpatrick +5 more
TL;DR: It is demonstrated that Arabidopsis thaliana has two functional homologs of PDX1 and a single homolog ofPDX2, and it is reported that the single PDX2 homolog is essential for plant viability.
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Two independent routes of de novo vitamin B6 biosynthesis: not that different after all.
Thérésa Bridget Fitzpatrick,Nikolaus Amrhein,Barbara Kappes,Peter Macheroux,Ivo Tews,Thomas Raschle +5 more
TL;DR: In this article, the authors compare the two independent pathways to the biosynthesis of vitamin B6 and reveal that the key biosynthetic enzymes of both pathways are, in fact, very similar both structurally and mechanistically.
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Structural and Functional Characterization of the Integral Membrane Protein VDAC-1 in Lipid Bilayer Nanodiscs
TL;DR: The ability to study integral membrane proteins at atomic resolution with solution NMR in phospholipid bilayers, rather than in detergent micelles, offers exciting novel possibilities to approach the biophysical properties of membrane proteins under nondenaturing conditions, which makes this technology particular suitable for protein-protein interactions and other functional studies.
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On the Two Components of Pyridoxal 5′-Phosphate Synthase from Bacillus subtilis
TL;DR: This report corroborates a recent report on the identification of the substrates of YaaD and provides unequivocal proof of the identity of the reaction product and reports on the detailed characterization of the inhibition of the glutaminase domain, and thus PLP synthesis, by the glutamine analog acivicin.