Author

D. L. Theobald

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biochemistry· 2 Evolutionary Biology· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:protein structure· 3 Research Focus:protein folding & dynamics· 2 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Organism:mouse· 1 Assay:protein sequence· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

C. Norn· 1 shared C. Xu· 1 shared H. M. Frank· 1 shared I. Andre· 1 shared J. D. Wirth· 1 shared J. I. Boucher· 1 shared K. A. Mackin· 1 shared P. A. Garrity· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 10 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperEvolutionary Biology

C. Norn

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structure of an insect gustatory receptor

H. M. Frank, S. Walujkar, R. M. Walsh, W. J. Laursen, D. L. Theobald, P. A. Garrity, R. Gaudet

The paper determines the structure of BmGr9, an insect gustatory receptor, and compares it to olfactory receptors to understand ligand specificity.

bioRxiv · Dec 19, 2023Biochemistry

Stability of Alternative Bacteriorhodopsin Folds

K. A. Mackin, D. L. Theobald

The paper assesses the stability of altered bacteriorhodopsin folds and finds that structural changes do not critically destabilize the protein, though extinction coefficients vary independently.

bioRxiv · Jun 21, 2023 · PreprintBiochemistry

Strong epistasis constrains the evolution of strict substrate specificity in apicomplexan lactate dehydrogenases

J. D. Wirth, J. I. Boucher, C. Xu, S. Classen, D. L. Theobald

This study investigates the evolution of substrate specificity in apicomplexan lactate dehydrogenases, revealing strong epistasis that constrains evolutionary changes and limits reversion to ancestral phenotypes.

bioRxiv · Jun 21, 2023 · PreprintEvolutionary Biology

A thermodynamic model of protein structure evolution explains empirical amino acid rate matrices

C. Norn, I. Andre, D. L. Theobald

The paper develops a thermodynamic model to explain amino acid substitution rates by integrating protein stability and genetic code constraints, accurately replicating empirical rate matrices.

bioRxiv · Dec 2, 2020 · PreprintEvolutionary Biology