Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensional <sup>1</sup> H-detected solid-state NMR
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- Alexander Klein
- Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
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- Petra Rovó
- Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
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- Varun V. Sakhrani
- Department of Chemistry, University of California, Riverside, CA 92521
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- Yangyang Wang
- Department of Chemistry, University of California, Riverside, CA 92521
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- Jacob B. Holmes
- Department of Chemistry, University of California, Riverside, CA 92521
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- Viktoriia Liu
- Department of Chemistry, University of California, Riverside, CA 92521
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- Patricia Skowronek
- Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
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- Laura Kukuk
- Department of Chemistry and Chemical Biology, TU Dortmund University, 44227 Dortmund, Germany
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- Suresh K. Vasa
- Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
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- Peter Güntert
- Institute of Biophysical Chemistry, Goethe University, 60438 Frankfurt am Main, Germany
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- Leonard J. Mueller
- Department of Chemistry, University of California, Riverside, CA 92521
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- Rasmus Linser
- Department of Chemistry and Pharmacy, Ludwig Maximilians University, 81377 Munich, Germany
Description
<jats:title>Significance</jats:title> <jats:p>The atomic-level understanding of protein function and enzyme catalysis requires site-specific information on chemical properties such as protonation and hybridization states and chemical exchange equilibria. This information is encoded in NMR chemical shifts, which serve as important complementary information to structural data from other experimental techniques or structure prediction algorithms. This study demonstrates that comprehensive chemical-shift assignments are achievable for large and highly complex proteins, offering insights into chemical structure and dynamics. The access to the active-site chemistry in the 144-kDa (72-kDa asymmetric unit) enzyme tryptophan synthase demonstrated here extends the elucidation of chemical properties to a member of an important class of enzymes of interest in pharmacology and biotechnology.</jats:p>
Journal
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 119 (4), 2022-01-20
Proceedings of the National Academy of Sciences
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Details 詳細情報について
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- CRID
- 1360857593777131264
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- ISSN
- 10916490
- 00278424
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- Data Source
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- Crossref
- KAKEN