Author

Richard D. Whitehead

University of ConnecticutORCID 0000-0001-5918-1908Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 1 Biophysics· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

Andrei T. AlexandrescuiD· 3 shared Alia Hassan· 1 shared Angela M. GronenborniD· 1 shared Antonio J. RuaiD· 1 shared Carolyn M. TeschkeiD· 1 shared Changmiao GuoiD· 1 shared Gal Porat‐DahlerbruchiD· 1 shared Jochem O. StruppeiD· 1 shared

Activity by Year

2023-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersBiophysics

Andrei T. AlexandrescuORCID

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3 papers

Recent·Most cited

Solution structure of the Z0 domain from transcription repressor BCL11A sheds light on the sequence properties of protein-binding zinc-fingers

Rilee E. Harris, Richard D. Whitehead, Andrei T. Alexandrescu

The paper determines the solution structure of the Z0 domain of BCL11A and identifies sequence patterns distinguishing DNA-binding from non-binding zinc-fingers.

Protein Science · Mar 18, 2025Peer-reviewedBiophysics

Structural Model of Bacteriophage P22 Scaffolding Protein in a Procapsid by Magic-Angle Spinning NMR

Changmiao Guo, Richard D. Whitehead, Jochem O. Struppe, Gal Porat‐Dahlerbruch, Alia Hassan, Angela M. Gronenborn, Andrei T. Alexandrescu, Carolyn M. Teschke, Tatyana E. Polenova

This study determines the structure of bacteriophage P22 scaffolding protein within its procapsid using magic-angle spinning NMR, revealing a trimer of dimers with both helical and disordered regions.

bioRxiv · Nov 1, 2024 · PreprintBiochemistry

NMR structure verifies the eponymous degenerate zinc finger domain of transcription factor ZNF750

Antonio J. Rua, Richard D. Whitehead, Andrei T. Alexandrescu

The paper uses NMR to show that the degenerate ZNF domain of ZNF750 binds Zn2+ with high affinity and forms a structured ββ fold, challenging the assumption that degenerate ZNFs are disordered.

bioRxiv · Jun 10, 2023 · PreprintMolecular Biology