Author

C. P. Owens

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· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:bacteria (other)· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell type annotation· 1 Assay:protein structure· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Kliman· 1 shared A. S. Ramaswamy· 1 shared A. Tajii· 1 shared B. T. Dinn· 1 shared D. L. Willard· 1 shared D. Ly· 1 shared E. Y. Wong· 1 shared G. Fumes· 1 shared

Activity by Year

2023-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 18 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 paperBiochemistry

A. Kliman

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivAug 25, 2023

Mutational analysis of the nitrogenase carbon monoxide protective protein CowN reveals that a conserved C-terminal glutamic acid residue is necessary for its activity

D. L. Willard, J. J. Arellano, M. Underdahl…·C. P. Owens

This study identifies a conserved glutamic acid residue in CowN essential for its function in protecting nitrogenase from CO inhibition and binding to nitrogenase.

DOI 10.1021/acs.biochem.3c00421

experimental assay

𝕏 PostBluesky

BiochemistrybioRxivPreprintMay 30, 2023

Uncovering structural features that control substrate specificity in a Lactobacillus chlorogenic acid esterase

K. K. Omori, T. L. S. Okumura, N. B. Carl…·C. P. Owens

This study identifies a Lys residue in an extended loop that determines substrate specificity in a Lactobacillus chlorogenic acid esterase by hydrogen bonding to chlorogenic acid.

DOI 10.1101/2023.05.30.542953

bacteria (other)structural biology

𝕏 PostBluesky

BiochemistrybioRxivPreprintMay 30, 2023

Purification and biochemical characterization of the DNA binding domain of the nitrogenase transcriptional activator NifA from Gluconacetobacter diazotrophicus

H. G. Standke, L. Kim, C. P. Owens

This study investigates the role of a Cys pair in the DNA binding domain of Gd-NifA, finding it does not regulate DNA binding or dimerization through redox changes.

DOI 10.1101/2023.05.30.542961

bacteria (other)protein structure

𝕏 PostBluesky