Author

L. J. Mueller

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:structural biology· 1

Frequent Co-Authors

V. Liu· 2 shared A. D. Gill· 1 shared A. Hassan· 1 shared A. Klein· 1 shared B. G. Caulkins· 1 shared B. Perrone· 1 shared C.-e. A. Chang· 1 shared E. Hilario· 1 shared

Activity by Year

2021-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiophysics

V. Liu

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2 papers

Recent·Most cited

Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate

J. B. Holmes, V. Liu, B. G. Caulkins, E. Hilario, R. K. Ghosh, V. N. Drago, R. P. Young, J. Romero, A. D. Gill, P. M. Bogie, J. Paulino, X. Wang, G. Riviere, Y. K. Bosken, J. Struppe, , L. J. Mueller

This paper uses NMR-assisted crystallography to determine the protonation states and structure of the tryptophan synthase α-aminoacrylate intermediate, revealing insights into its reactivity and catalytic mechanism.

Proceedings of the National Academy of Sciences · Jan 7, 2022Peer-reviewedBiophysics

Residue-specific insights into (2x)72 kDa tryptophan synthase obtained from fast-MAS 1H-detected solid-state NMR

A. Klein, P. Rovó, V. V. Sakhrani, Y. Wang, J. Holmes, V. Liu, P. Skowronek, L. Kukuk, S. K. Vasa, P. Güntert, L. J. Mueller, R. Linser

This study uses solid-state NMR to characterize a 72 kDa tryptophan synthase, overcoming size limitations and providing insights into catalytic residues.

bioRxiv · May 12, 2021 · PreprintBiochemistry