Author

A. C. K. Chan

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· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Organism:C. elegans· 1 Approach:experimental assay· 1 Assay:protein structure· 1 Assay:structural biology· 1

Frequent Co-Authors

M. E. P. Murphy· 2 shared C. S.-H. Lin· 1 shared F. Jabbarpour· 1 shared I. Rajkovic· 1 shared I. Y. Yen· 1 shared J. Herrmann· 1 shared J. Smit· 1 shared L. Shapiro· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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2 shared papersBiochemistry

M. E. P. Murphy

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2 papers

Recent·Most cited

Mechanism of the CBM35 domain in assisting catalysis by Ape1, a Campylobacter jejuni O-acetyl esterase

C. S.-H. Lin, I. Y. Yen, A. C. K. Chan, M. E. P. Murphy

This study identifies the role of the CBM35 domain in enhancing catalytic efficiency of Ape1, a de-O-acetylase from Campylobacter jejuni, through structural and biochemical analyses.

bioRxiv · Sep 23, 2021 · PreprintBiochemistry

A Bacterial Surface Layer Protein Exploits Multi-step Crystallization for Rapid Self-assembly

J. Herrmann, P.-N. Li, F. Jabbarpour, A. C. K. Chan, I. Rajkovic, T. Matsui, L. Shapiro, J. Smit, T. Weiss, M. E. P. Murphy, S. Wakatsuki

This paper shows a bacterial surface layer protein uses a multi-step pathway with a nucleation domain to rapidly crystallize, enabling efficient 2D self-assembly on cell surfaces.

Proceedings of the National Academy of Sciences · Dec 17, 2019Peer-reviewedBiophysics