Author

E. J. Stollar

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· 3

Signature Assays, Organisms & Methods

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Approach:mechanistic / dynamical model· 3 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 2 Organism:yeast· 2 Assay:proteomics· 1

Frequent Co-Authors

K. A. Ball· 3 shared R. Stix· 2 shared A. Connor· 1 shared A. H. Carhart· 1 shared A. J. Adkins· 1 shared B. J. Lantz· 1 shared E. Masoumzadeh· 1 shared G. J. Gerlach· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiophysics

K. A. Ball

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3 papers

Recent·Most cited

How a highly acidic SH3 domain folds in the absence of its charged peptide target

V. Jaramillo- Martinez, M. J. Dominguez, G. M. Bell, M. E. Souness, A. H. Carhart, M. A. Cuibus, E. Masoumzadeh, B. J. Lantz, A. J. Adkins, M. P. Latham, K. A. Ball, E. J. Stollar

This study investigates how a highly acidic yeast SH3 domain folds despite electrostatic repulsion, showing that salt stabilizes it and hydrophobic collapse offsets repulsion during folding.

bioRxiv · Mar 21, 2023Biophysics

Gaussian accelerated molecular dynamics reveals that a proline-rich signaling peptide frequently samples cis conformations when unbound

J. Alcantara, R. Stix, K. Huang, A. Connor, R. East, V. Jaramillo-Martinez, E. J. Stollar, K. A. Ball

This study uses Gaussian accelerated molecular dynamics to simulate proline isomerization in proline-rich peptides, finding that cis conformations are frequently sampled and affect structural properties and binding potential.

bioRxiv · Jul 1, 2021Biophysics

A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway

G. J. Gerlach, R. Carrock, R. Stix, E. J. Stollar, K. A. Ball

This study uses molecular dynamics simulations to show that the SH3 domain binding pathway of the yeast Abp1p involves a flexible encounter complex stabilized by hydrophobic and electrostatic interactions.

PLOS Computational Biology · Sep 14, 2020Peer-reviewedBiophysics