Author

Robert V. Williams

University of Massachusetts AmherstORCID 0000-0003-1839-6122Unclaimed 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 Assay:protein structure· 2 Approach:deep learning· 1 Organism:E. coli· 1

Frequent Co-Authors

Lila M. GieraschiD· 2 shared Akshitha MaqtedariD· 1 shared Daniel N. HebertiD· 1 shared Eugenia M. CléricoiD· 1 shared Kevin P. GuayiD· 1 shared María-Agustina RossiiD· 1 shared Owen A. Hurlbut LeskiD· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

7 top collaborators · 12 mutual co-author links

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2 shared papersBiochemistry

Lila M. GieraschORCID

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2 papers

Recent·Most cited

BiochemistryJournal of Biological ChemistryPeer-reviewedOct 1, 2026

The cysteine-rich domain of SEP15, a selenoprotein co-chaperone of the ER chaperone, UDP-glucose:glycoprotein glucosyltransferase, adopts a novel fold

Robert V. Williams, Kevin P. Guay, Owen A. Hurlbut Lesk…·Lila M. Gierasch

The paper determines the structure of the cysteine-rich domain of SEP15 using AlphaFold and NMR, revealing a novel helical fold stabilized by disulfide bonds.

DOI 10.1016/j.jbc.2026.113629

protein structuredeep learning

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BiochemistryJournal of Biological ChemistryPeer-reviewedJan 20, 2026

The nucleotide exchange factor, GrpE, modulates substrate affinity by interaction of its N-terminal tails with the DnaK substrate-binding domain.

Akshitha Maqtedar, María-Agustina Rossi, Eugenia M. Clérico…·Lila M. Gierasch

This paper investigates how GrpE modulates DnaK's substrate affinity through interactions between GrpE's N-terminal tails and DnaK's SBD, revealing a temperature-dependent mechanism.

DOI 10.1016/j.jbc.2026.111176

E. coliprotein structure

𝕏 PostBluesky