Author

J. Weresczczynski

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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Research Focus:chromatin & epigenetic regulation· 3 Approach:mechanistic / dynamical model· 3 Organism:bacteria (other)· 1 Assay:ChIP-seq· 1 Approach:experimental assay· 1 Assay:Hi-C· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. I. Greenwood· 1 shared A. Rice· 1 shared C. A. Musselman· 1 shared D. C. Woods· 1 shared E. A. Morrison· 1 shared H. Kohestani· 1 shared L. Baweja· 1 shared M. Cotten· 1 shared

Activity by Year

2020-2020 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiophysics

A. I. Greenwood

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4 papers

Recent·Most cited

Nucleosome composition regulates the histone H3 tail conformational ensemble and accessibility

E. A. Morrison, L. Baweja, M. G. Poirier, J. Weresczczynski, C. A. Musselman

This study examines how nucleosome composition affects the conformational dynamics and accessibility of the H3 histone tail in hexasomes and tetrasomes.

bioRxiv · Jun 26, 2020Biophysics

Effects of H2A.B incorporation on nucleosome structures and dynamics

H. Kohestani, J. Weresczczynski

This study uses molecular dynamics simulations to show that H2A.B incorporation reduces nucleosome compactness by weakening protein-DNA and protein-protein interactions, increasing DNA accessibility and transcription.

bioRxiv · Jun 25, 2020Biophysics

Elucidating the Influence of Linker Histone Variants on Chromatosome Dynamics and Energetics

D. C. Woods, J. Weresczczynski

This study uses molecular dynamics simulations to compare how two linker histone variants affect chromatosome structure, energetics, and dynamics, revealing differences in their binding preferences and thermodynamic efficiency.

bioRxiv · Feb 25, 2020Biophysics

Lipopolysaccharide Simulations are Sensitive to Phosphate Charge and Ion Parameterization

A. Rice, M. T. Rooney, A. I. Greenwood, M. Cotten, J. Weresczczynski

This study shows that LPS simulations are sensitive to phosphate charge and ion parameterization, with protonated LPS and specific cations providing better agreement with experiments.

bioRxiv · Jan 22, 2020Biophysics