T
Thomas Szyperski
Researcher at University at Buffalo
Publications - 201
Citations - 11760
Thomas Szyperski is an academic researcher from University at Buffalo. The author has contributed to research in topics: Structural genomics & Nuclear magnetic resonance spectroscopy. The author has an hindex of 55, co-authored 195 publications receiving 11192 citations. Previous affiliations of Thomas Szyperski include Rutgers University & State University of New York System.
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Consistent blind protein structure generation from NMR chemical shift data
Yang Shen,Oliver F. Lange,Frank Delaglio,Paolo Rossi,James M. Aramini,Gaohua Liu,Alexander Eletsky,Yibing Wu,Kiran Kumar Singarapu,Alexander Lemak,Alexandr Ignatchenko,Cheryl H. Arrowsmith,Thomas Szyperski,Gaetano T. Montelione,David Baker,Ad Bax +15 more
TL;DR: The chemical shift based structure determination protocol uses an empirically optimized procedure to select protein fragments from the Protein Data Bank, in conjunction with the standard ROSETTA Monte Carlo assembly and relaxation methods, and potentially provides a new direction for high-throughput NMR structure determination.
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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling.
TL;DR: Experience gained with the present project and a previous application of the same principles with the cyclic polypeptide cyclosporin A provides a basis for the selection of the optimal NMR experiments to be used in conjunction with biosynthetic fractional 13C labeling of proteins and peptides.
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Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism.
Uwe Sauer,Daniel R Lasko,Jocelyne Fiaux,Michel Hochuli,Ralf W. Glaser,Thomas Szyperski,Kurt Wüthrich,James E. Bailey +7 more
TL;DR: Data indicate remarkable robustness and rigidity in central carbon metabolism in the presence of genetic variation and more significant physiological changes and flux ratio differences were seen in response to altered environmental conditions.
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Biosynthetically directed fractional 13C-labeling of proteinogenic amino acids. An efficient analytical tool to investigate intermediary metabolism.
TL;DR: Biosynthetically directed fractional 13C labeling of amino acids provides an efficient analytical tool to quantitatively investigate glycolysis, pyruvate metabolism, pentose phosphate pathway, tricarboxylic acid cycle and C1 metabolism.
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GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information
Seho Kim,Thomas Szyperski +1 more
TL;DR: GFT NMR opens new avenues to establish high-throughput protein structure determination, to investigate systems with a higher degree of chemical shift degeneracy, and to study dynamic phenomena such as slow folding of biological macromolecules in greater detail.