Author

K. A. Ball

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 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:mechanistic / dynamical model· 4 Research Focus:protein folding & dynamics· 4 Assay:protein structure· 3 Approach:experimental assay· 2 Assay:proteomics· 2 Organism:yeast· 2 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

E. J. Stollar· 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 D. J. Stanley· 1 shared E. Masoumzadeh· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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3 shared papersBiophysics

E. J. Stollar

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Author profile →

5 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

Rapid discovery of drug target engagement by isothermal shift assay

K. J. Webb, K. A. Ball, S. J. Coleman, J. Jacobsen, M. Stowell, W. M. Old

The paper introduces iTSA, an isothermal shift assay for rapid drug target identification, showing higher throughput and multiplexing compared to thermal proteome profiling.

bioRxiv · Apr 5, 2019 · PreprintPharmacology & Toxicology

Conformational dynamics of the HIV Vif protein complex

K. A. Ball, L. M. Chan, D. J. Stanley, E. Tierney, S. Thapa, H. M. Ta, L. A. Burton, J. M. Binning, M. Jacobsen, J. Gross

This study uses MD simulations and NMR to analyze the conformational dynamics of the HIV Vif protein complex, showing global motions in the VCBC complex and a more static structure when bound to CUL5.

bioRxiv · Nov 29, 2018Biophysics