Author

A. Bitran

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

Research Focus:protein folding & dynamics· 4 Approach:experimental assay· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1 Organism:E. coli· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

E. Shakhnovich· 3 shared E. Serebryany· 2 shared K. Park· 2 shared W. M. Jacobs· 2 shared B. Budnik· 1 shared E. I. Shakhnovich· 1 shared S. A. Trauger· 1 shared V. Y. Zhao· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

9 top collaborators · 20 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

3 shared papersBiophysics

E. Shakhnovich

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Cotranslational formation of disulfides guides folding of the SARS CoV-2 receptor binding domain

A. Bitran, K. Park, E. Serebryany, E. Shakhnovich

The paper investigates how disulfide bond formation during translation guides the folding of the SARS-CoV-2 RBD, showing that non-equilibrium mechanisms are required to prevent misfolding.

bioRxiv · Nov 10, 2022Biophysics

Systematic conformation-to-phenotype mapping via limited deep-sequencing of proteins

E. Serebryany, V. Y. Zhao, K. Park, A. Bitran, S. A. Trauger, B. Budnik, E. I. Shakhnovich

The paper develops a method to map protein conformations to phenotypes by systematically analyzing disulfide bonds in proteins.

bioRxiv · Apr 12, 2022Biophysics

DBFOLD: An efficient algorithm for computing folding pathways of complex proteins

A. Bitran, W. M. Jacobs, E. Shakhnovich

DBFOLD predicts protein folding pathways and transition rates by combining Monte-Carlo simulations with high-temperature unfolding simulations to account for non-native interactions.

bioRxiv · Sep 9, 2020Biophysics

Co-translational folding allows misfolding-prone proteins to circumvent deep kinetic traps

A. Bitran, W. M. Jacobs, X. Zhai, E. Shakhnovich

This paper shows co-translational folding helps misfolding-prone proteins avoid kinetic traps by optimizing nascent chain lengths and translation rates.

bioRxiv · Aug 1, 2019Biophysics