Author

B. M. Rubenstein

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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Biophysics· 2

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Assay:protein structure· 1

Frequent Co-Authors

C. S. Wylie· 1 shared D. C. Dalgarno· 1 shared D. M. Weinreich· 1 shared F. M. Ytreberg· 1 shared G. Monteiro da Silva· 1 shared J. Huang· 1 shared J. S. Patel· 1 shared J. Yang· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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1 shared paperBiophysics

C. S. Wylie

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2 papers

Recent·Most cited

Compound Mutations in the Abl1 Kinase Cause Inhibitor Resistance by Shifting DFG Flip Mechanisms and Relative State Populations

G. Monteiro da Silva, K. Lam, D. C. Dalgarno, B. M. Rubenstein

This study uses Weighted Ensemble simulations to analyze DFG flip mechanisms in Abl1 kinase and shows how compound mutations increase free energy barriers, leading to inhibitor resistance.

bioRxiv · May 23, 2024 · PreprintBiophysics

Predicting the Viability of Beta-Lactamase: How Folding and Binding Free Energies Correlate with Beta-Lactamase Fitness

J. Yang, N. Naik, J. S. Patel, C. S. Wylie, W. Gu, J. Huang, F. M. Ytreberg, M. T. Naik, D. M. Weinreich, B. M. Rubenstein

This paper evaluates how well thermodynamic folding and binding free energies predict the fitness of beta-lactamase mutants using experimental data and computational models.

bioRxiv · Apr 15, 2020Biophysics