Author

Rebecca M. Lang Harman

Augusta University

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 Bioengineering· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Approach:experimental assay· 1

Frequent Co-Authors

Shogo MoriiD· 2 shared Angela C. SpenceriD· 1 shared Anna Parviainen· 1 shared D. Brooks Dickson· 1 shared Daniela Figueredo· 1 shared Favor O. Aruna· 1 shared Gracie Blackstone· 1 shared H. Grace Blackstone· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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2 shared papersBiochemistry

Shogo MoriORCID

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2 papers

Recent·Most cited

BiochemistrybioRxivPreprintJun 19, 2026

High side chain promiscuity of the terminal enzyme in the homologation pathway for L-phenylalanine and L-tyrosine

Rebecca M. Lang Harman, H. Grace Blackstone, Juan-Paolo Reynes…·Shogo Mori

This study investigates the substrate promiscuity of the enzyme HphB in the homologation pathway, showing it can accept diverse side chains while maintaining backbone specificity.

DOI 10.64898/2026.06.15.732371

biophysical modelingprotein folding & dynamics

𝕏 PostBluesky

BioengineeringbioRxivPreprintDec 3, 2025

Amenability to Engineering of the Homologation Enzyme, HphA, through Homologous-Based Site-Directed Mutagenesis

Rebecca M. Lang Harman, Gracie Blackstone, Favor O. Aruna…·Shogo Mori

This study identifies key residues in HphA that influence substrate specificity through site-directed mutagenesis, showing that the A73L mutation broadens its substrate range.

DOI 10.64898/2025.12.01.691582

experimental assayprotein folding & dynamics

𝕏 PostBluesky