Author

W. Sheffler

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· 4 Bioengineering· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:deep learning· 6 Assay:protein structure· 6 Approach:statistical model· 4 Research Focus:drug response / drug discovery· 3 Approach:experimental assay· 3 Research Focus:protein design· 3 Research Focus:protein structure prediction· 2 Organism:E. coli· 1

Frequent Co-Authors

D. Baker· 6 shared N. P. King· 4 shared A. Khmelinskaia· 3 shared Y. Hsia· 3 shared A. J. Borst· 2 shared A. K. Bera· 2 shared A. Kang· 2 shared C. M. Chow· 2 shared

Activity by Year

2017-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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6 shared papersBiochemistry

D. Baker

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

Computational design of non-porous, pH-responsive antibody nanoparticles

E. C. Yang, R. Divine, M. C. Miranda, A. J. Borst, W. Sheffler, J. Z. Zhang, J. Decarreau, A. Sarajovi, M. Abedi, N. Goldbach, M. Ahlrichs, C. Dobbins, A. Hand, S. Cheng, M. Lamb, , D. Baker

This paper designs pH-responsive antibody nanoparticles with three distinct protein components that disassemble at tunable pH levels, enabling targeted delivery of biologics.

bioRxiv · Apr 17, 2023Bioengineering

De novo design of modular peptide binding proteins by superhelical matching

K. Wu, H. Bai, Y.-T. Chang, R. Redler, K. E. McNally, W. Sheffler, T. Brunette, D. R. Hicks, T. E. Morgan, T. J. Stevens, A. Broerman, I. Goreshnik, M. DeWitt, C. M. Chow, Y. Shen, , D. Baker

This paper introduces a method to design modular peptide binding proteins that bind repeating peptide sequences with high specificity and affinity.

bioRxiv · Nov 14, 2022 · PreprintBiochemistry

Fast and versatile sequence-independent protein docking for nanomaterials design using RPXDock

W. Sheffler, E. C. Yang, Q. Dowling, Y. Hsia, C. N. Fries, J. Stanislaw, M. Langowski, M. Brandys, A. Khmelinskaia, N. P. King, D. Baker

RPXDock enables fast, flexible protein docking for symmetric architectures, supporting diverse applications in nanomaterial design.

bioRxiv · Oct 25, 2022Bioengineering

Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains

J. Y. Wang, A. Khmelinskaia, W. Sheffler, M. C. Miranda, A. Antanasijevic, A. J. Borst, S. V. Torres, C. Shu, Y. Hsia, U. Nattermann, D. Ellis, C. Walkey, M. Ahlrichs, S. Chan, A. Kang, , N. P. King

This study identifies cryptic transmembrane domains in designed protein nanoparticles that hinder secretion and introduces a computational tool, Degreaser, to remove them while maintaining stability, improving secretion efficiency.

bioRxiv · Aug 4, 2022Biochemistry

Designed proteins assemble antibodies into modular nanocages

R. Divine, H. V. Dang, G. Ueda, J. A. Fallas, I. Vulovic, W. Sheffler, S. Saini, Y. T. Zhao, I. X. Raj, P. A. Morawski, M. F. Jennewein, L. J. Homad, Y.-H. Wan, M. R. Tooley, F. Seeger, , D. Baker

The paper designs modular nanocages that assemble antibodies into precise geometries, enhancing signaling and neutralization compared to free antibodies.

bioRxiv · Dec 1, 2020Biochemistry

Hierarchical design of multi-scale protein complexes by combinatorial assembly of oligomeric helical bundle and repeat protein building blocks

Y. Hsia, R. Mout, W. Sheffler, N. I. Edman, I. Vulovic, Y.-J. Park, R. L. Redler, M. J. Bick, A. K. Bera, A. Courbet, A. Kang, T. Brunette, U. Nattermann, E. Tsai, A. Saleem, , D. Baker

This paper describes a hierarchical method to design multi-scale symmetric protein complexes using repeat proteins and helical bundles, resulting in large symmetric assemblies like an icosahedral nanocage.

bioRxiv · Jul 27, 2020Biochemistry

Efficient Flexible Backbone Protein-Protein Docking for Challenging Targets

N. A. Marze, S. S. Roy Burman, W. Sheffler, J. J. Gray

This paper introduces a new protein-protein docking method that efficiently samples flexible backbone conformations and achieves higher success rates for docking flexible complexes.

bioRxiv · Nov 22, 2017Biophysics