Author

B. S. Schuster

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Approach:mechanistic / dynamical model· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1 Assay:protein sequence· 1

Frequent Co-Authors

B. Favetta· 2 shared F. M. Kelley· 2 shared J. Mittal· 2 shared A. Rizuan· 1 shared A. RIZVI· 1 shared C. G. Garcia· 1 shared D. Milovanovic· 1 shared H. Wang· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiophysics

B. Favetta

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Author profile →

4 papers

Recent·Most cited

Revealing nanoscale structure and interfaces of protein and polymer condensates via cryo-electron microscopy

A. RIZVI, B. Favetta, N. Jaber, Y.-k. Lee, J. Jiang, N. Idris, B. S. Schuster, W. Dai, J. P. Patterson

This study uses cryo-EM to analyze nanoscale structures of protein and polymer condensates, revealing core-shell morphologies and internal inhomogeneities.

bioRxiv · Feb 15, 2024 · PreprintBiophysics

Expanding the molecular language of protein liquid-liquid phase separation

S. Rekhi, C. G. Garcia, M. Barai, A. Rizuan, B. S. Schuster, K. L. Kiick, J. Mittal

This study explores how amino acid sequences influence protein liquid-liquid phase separation and material properties of condensates through systematic sequence manipulations and molecular simulations.

bioRxiv · Mar 2, 2023Biophysics

More than just oil droplets in water: surface tension and viscosity of protein condensates quantified by micropipette aspiration

H. Wang, F. M. Kelley, D. Milovanovic, B. S. Schuster, Z. Shi

This paper develops a micropipette-based technique to quantify surface tension and viscosity of biomolecular condensates without labeling or surface wetting effects, demonstrating its accuracy with LAF-1 RGG domains and ATPS.

bioRxiv · May 28, 2021Biophysics

Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants

F. M. Kelley, B. Favetta, R. M. Regy, J. Mittal, B. S. Schuster

The paper investigates how amphiphilic proteins influence the structure and size of biomolecular condensates by forming surface layers and multiphasic structures.

bioRxiv · May 28, 2021Biophysics