Author

P. Hinchliffe

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· 2

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Approach:mechanistic / dynamical model· 1 Assay:protein structure· 1

Frequent Co-Authors

A. J. Mulholland· 2 shared C. L. Tooke· 2 shared J. Spencer· 2 shared M. Beer· 2 shared A. S. F. Oliveira· 1 shared A. T. Y. Li· 1 shared B. Balega· 1 shared C. J. Schofield· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBiochemistry

A. J. Mulholland

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2 papers

Recent·Most cited

Dynamical Responses Predict a Distal Site that Modulates Activity in an Antibiotic Resistance Enzyme

M. Beer, A. S. F. Oliveira, C. L. Tooke, P. Hinchliffe, A. T. Y. Li, B. Balega, J. Spencer, A. J. Mulholland

The paper uses dynamical simulations and experiments to identify a distal site in an antibiotic resistance enzyme that modulates activity when mutated.

bioRxiv · Apr 29, 2024Biochemistry

Tautomer-specific deacylation and {Omega}-loop flexibility explain carbapenem-hydrolyzing, broad-spectrum activity of the KPC-2 β-lactamase

C. L. Tooke, P. Hinchliffe, M. Beer, K. Zinovjev, C. K. Colenso, C. J. Schofield, A. J. Mulholland, J. Spencer

This study identifies how tautomer-specific deacylation and {Omega}-loop flexibility enable KPC-2 β-lactamase to efficiently hydrolyze carbapenems, revealing structural and energetic mechanisms for its broad-spectrum activity.

bioRxiv · Nov 11, 2022Biochemistry