Author

B. J. Hilbert

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· 4 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:structural biology· 3 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

B. A. Kelch· 4 shared N. P. Stone· 3 shared J. A. Hayes· 2 shared A. Majewski· 1 shared A. Nair· 1 shared C. Duffy· 1 shared C. Gaubitz· 1 shared D. Hidalgo· 1 shared

Activity by Year

2016-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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4 shared papersBiochemistry

B. A. Kelch

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Author profile →

5 papers

Recent·Most cited

Viral Packaging ATPases Utilize a Glutamate Switch to Couple ATPase Activity and DNA Translocation

J. Pajak, R. Atz, B. J. Hilbert, M. Morais, B. A. Kelch, P. Jardine, G. Arya

This study identifies a glutamate switch mechanism in viral packaging ATPases that couples ATP binding to DNA translocation through conformational changes.

bioRxiv · Dec 1, 2020Biophysics

The ΔF508 CFTR defect: molecular mechanism of suppressor mutation V510D and the contribution of transmembrane helix unraveling

K. S. Simon, K. Nagarajan, I. Mechin, C. Duffy, P. Manavalan, S. Altmann, A. Majewski, J. Foley, J. S. Kaczmarek, S. Bercury, M. Maderia, B. J. Hilbert, J. D. Batchelor, R. Ziegler, J. Bajko, , G. D. Hurlbut

This study investigates the molecular mechanism of the ΔF508 CFTR mutation and how suppressor mutations like V510D and R1070W rescue its function by preventing transmembrane helix unraveling.

bioRxiv · Apr 19, 2020 · PreprintBiochemistry

A thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry

J. A. Hayes, B. J. Hilbert, C. Gaubitz, N. P. Stone, B. A. Kelch

This paper identifies and characterizes the TerS protein of bacteriophage P74-26, revealing its unique structural features and functional roles in DNA binding and TerL interaction.

bioRxiv · Nov 21, 2019Biochemistry

A hyperthermophilic phage decoration protein suggests common evolutionary origin with Herpesvirus Triplex proteins and an anti-CRISPR protein

N. P. Stone, B. J. Hilbert, D. Hidalgo, K. T. Halloran, B. A. Kelch

The paper investigates the structure and stability of a capsid protein from a hyperthermophilic phage, revealing its evolutionary relationship with herpesvirus triplex proteins and an anti-CRISPR protein.

bioRxiv · Nov 13, 2017Biochemistry

The large terminase DNA packaging motor grips DNA with its ATPase domain for cleavage by the flexible nuclease domain

B. J. Hilbert, J. A. Hayes, N. P. Stone, R.-G. Xu, B. A. Kelch

This study investigates how the large terminase protein binds and cleaves DNA during viral genome packaging, revealing the ATPase domain's role in DNA binding and the nuclease domain's role in cleavage.

bioRxiv · Oct 19, 2016Biochemistry