Author

Chandrima Majumdar

University of California, BerkeleyORCID 0000-0002-6000-536XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Assay:protein sequence· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

Jamie H. D. CateiD· 2 shared Alanna SchepartziD· 1 shared Alexander Carlos SolivaniD· 1 shared Alexandra D. KentiD· 1 shared Douglas A. MitchelliD· 1 shared Hassane S. MchaourabiD· 1 shared J. R. VanceiD· 1 shared Katelyn A. Fitzgerald· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersBiochemistry

Jamie H. D. CateORCID

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2 papers

Recent·Most cited

Enzymatic formation of a conserved isoaspartate in ribosomal protein uS11

Yanqing Xue, Chandrima Majumdar, Salimat O. Sofela, Yekaterina Shulgina, Roma Nagle, Tianqi Wu, Hassane S. Mchaourab, Markus Voehler, Jamie H. D. Cate, Douglas A. Mitchell

The paper identifies an enzymatic pathway for isoaspartate formation in bacterial ribosomal protein uS11, showing its conservation and structural importance.

bioRxiv · Aug 27, 2026 · PreprintBiochemistry

Altering the ribosome exit tunnel to improve consecutive incorporation of challenging monomers

Alexandra D. Kent, Chandrima Majumdar, Katelyn A. Fitzgerald, Alexander Carlos Solivan, Martina Boga de Teresa, J. R. Vance, Alanna Schepartz, Jamie H. D. Cate

This study shows that an A2062U mutation in 23S rRNA improves ribosome activity for translating sequences with challenging monomers like proline and β2-hydroxy acids.

bioRxiv · Jun 2, 2026 · PreprintBiochemistry