Author

H. Worthy

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· 3

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:fluorescence / live-cell microscopy· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

D. Jones· 3 shared C. R. Pudney· 2 shared P. Rizkallah· 2 shared R. Johnson· 2 shared S. A. Wells· 2 shared S. Winter· 2 shared A. Barratt· 1 shared A. Embady· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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3 shared papersBiochemistry

D. Jones

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

N-linked glycosylation increases horse radish peroxidase rigidity leading to enhanced activity and stability.

K. Ramakrishnan, R. Johnson, S. Winter, H. Worthy, C. Thomas, D. Humer, O. Spadiut, S. Hindson, S. A. Wells, A. Barratt, G. Menzies, C. R. Pudney, D. Jones

This study shows glycosylation increases the rigidity of horseradish peroxidase, enhancing its activity and stability through structural changes.

bioRxiv · Sep 23, 2022 · PreprintBiochemistry

Structure and dynamics of a cold-active esterase reveals water entropy and active site accessibility as the likely drivers for cold-adaptation

N. Noby, H. Sabah Auhim, H. Worthy, S. Winter, A. Embady, H. Saeed, A. Hussein, C. Pudney, P. Rizkallah, S. A. Wells, D. Jones, C. R. Pudney

This study determines the structure of a cold-active esterase and identifies increased substrate accessibility and water entropy tolerance as the main drivers of its cold adaptation.

bioRxiv · Feb 23, 2021 · PreprintBiochemistry

The effect of proximity on the function and energy transfer capability of fluorescent protein pairs

J. Pope, R. Johnson, W. D. Jamieson, H. Worthy, S. Kailasam, H. Auhim, D. Watkins, P. Rizkallah, O. Castell, D. Jones

This study shows that dimerization of fluorescent protein pairs alters their fluorescent properties and FRET efficiency, challenging assumptions about FP-based proximity sensing.

bioRxiv · Nov 12, 2019 · PreprintBiochemistry