Author

C.-e. A. Chang

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 4

Signature Assays, Organisms & Methods

Click to filter · or open tag

Assay:protein structure· 3 Approach:deep learning· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:benchmarking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1

Frequent Co-Authors

S.-h. Chen· 2 shared T. I. Hung· 2 shared A. D. Gill· 1 shared A. Hassan· 1 shared B. Bhanu· 1 shared B. G. Caulkins· 1 shared B. Perrone· 1 shared E. Hilario· 1 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiophysics

S.-h. Chen

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Sampling Conformational Ensembles of Highly Dynamic Proteins via Generative Deep Learning

T. Ruzmetov, T. I. Hung, S. P. Jonnalagedda, S.-h. Chen, P. Fasihianifard, Z. Guo, B. Bhanu, C.-e. A. Chang

This paper introduces a deep learning model to sample conformational ensembles of dynamic proteins, demonstrating its ability to generate novel conformations and rationalize experimental findings.

bioRxiv · May 5, 2024Biophysics

PROTAC-induced Protein Structural Dynamics in Targeted Protein Degradation

K. Y. Wu, T. I. Hung, C.-e. A. Chang

This study computationally models PROTAC-induced protein dynamics to explain variation in degradation potency despite identical warheads.

bioRxiv · May 5, 2024Biophysics

Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate

J. B. Holmes, V. Liu, B. G. Caulkins, E. Hilario, R. K. Ghosh, V. N. Drago, R. P. Young, J. Romero, A. D. Gill, P. M. Bogie, J. Paulino, X. Wang, G. Riviere, Y. K. Bosken, J. Struppe, , L. J. Mueller

This paper uses NMR-assisted crystallography to determine the protonation states and structure of the tryptophan synthase α-aminoacrylate intermediate, revealing insights into its reactivity and catalytic mechanism.

bioRxiv · May 12, 2021Biophysics

Dissection of ligand-CDK8/CycC unbinding free energy barriers and kinetics by molecular simulations

Z. Tang, S.-H. Chen, C.-e. A. Chang

This paper uses molecular simulations to study ligand-CDK8/CycC unbinding kinetics and free energy barriers, guiding the design of ligands with improved residence time.

bioRxiv · Jun 22, 2019Biophysics