Author

S. A. Wells

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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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Assay:proteomics· 1 Approach:statistical model· 1 Assay:structural biology· 1

Frequent Co-Authors

C. R. Pudney· 3 shared D. Jones· 2 shared H. Worthy· 2 shared S. Winter· 2 shared A. Barratt· 1 shared A. Embady· 1 shared A. Hussein· 1 shared A. Kwok· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiochemistry

C. R. Pudney

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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

Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift

M. Knight, R. Woolley, A. Kwok, S. Parsons, H. Jones, C. Gulacsy, P. Phaal, O. Kassaar, K. Dawkins, E. Rodriguez, A. Marques, L. Bowsher, S. A. Wells, A. Watts, J. M. van den Elsen, , C. R. Pudney

This paper demonstrates that quantifying the fluorescence red edge excitation shift (REES) can sensitively monitor monoclonal antibody stability across timeframes and concentrations.

bioRxiv · Mar 23, 2020Biochemistry