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Alvar D. Gossert
Researcher at ETH Zurich
Publications - 49
Citations - 1681
Alvar D. Gossert is an academic researcher from ETH Zurich. The author has contributed to research in topics: Biology & Chemistry. The author has an hindex of 17, co-authored 42 publications receiving 1303 citations. Previous affiliations of Alvar D. Gossert include Novartis & University of Basel.
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A simple protocol for amino acid type selective isotope labeling in insect cells with improved yields and high reproducibility
Alvar D. Gossert,Alexandra Hinniger,Sascha Gutmann,Wolfgang Jahnke,André Strauss,César Fernández +5 more
TL;DR: By supplementing media with a well considered amount of yeast extract, similar protein amounts as with full media are obtained, without compromising on isotope incorporation, in single and dual amino acid labeling experiments incorporation ratios are consistently ≥90% for all amino acids tested.
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Prion protein NMR structures of elk and of mouse/elk hybrids
TL;DR: The NMR structure of the recombinant elk prion protein ( ePrP), which represents the cellular isoform (ePrPC) in the healthy organism, is described here and it is shown that the structured loop in ePrPC relates to these two local amino acid exchanges, so that mPrP[S170N,N174T] exactly mimics ePr PC.
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NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules.
Alvar D. Gossert,Wolfgang Jahnke +1 more
TL;DR: The concept of the validation cross is introduced, which helps to categorize experiments according to their information content and to simplify the choice of the right experiment in order to address a specific question.
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Exposing the Origins of Irreproducibility in Fluorine NMR Spectroscopy
TL;DR: It is demonstrated that internal referencing provides the most robust, practical, and reproducible method whereby chemical shifts can be consistently measured and confirmed between institutions to less than 30 ppb deviation.
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Nuclear magnetic resonance of hyperpolarized fluorine for characterization of protein-ligand interactions.
TL;DR: The ability to use a low ligand concentration permits the detection of ligands in slow exchange that are not easily amenable to drug screening by traditional NMR methods, and the relative speed and additional information gained may make the hyperpolarization-based approach an interesting alternative for use in drug discovery.