Author

M. H. Kolar

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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Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

A. C. Sanchez Rocha· 1 shared G. Nagy· 1 shared G. Zanchetta· 1 shared H. Grubmuller· 1 shared H. McGrath· 1 shared J. Kunkel· 1 shared K. Fujishima· 1 shared K. Hlouchova· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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1 shared paperBiophysics

A. C. Sanchez Rocha

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3 papers

Recent·Most cited

The interplay between peptides and RNA is critical for protoribosome compartmentalization and stability

S. Codispoti, T. Yamaguchi, M. Makarov, V. G. Giacobelli, M. Masek, M. H. Kolar, A. C. Sanchez Rocha, K. Fujishima, G. Zanchetta, K. Hlouchova

This paper investigates the role of ribosomal peptides in protoribosome compartmentalization and stability, showing that RNA-protein interactions protect RNA from degradation and influence structural flexibility.

bioRxiv · Jan 29, 2024Biophysics

Binding of the peptide deformylase on the ribosome surface modulates the structure and dynamics of the exit tunnel interior

H. McGrath, M. Cernekova, M. H. Kolar

The paper investigates how peptide deformylase (PDF) binding to the ribosome affects its structure and dynamics, showing long-range allosteric effects on the exit tunnel.

bioRxiv · Apr 20, 2022 · PreprintBiophysics

Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel

M. H. Kolar, G. Nagy, J. Kunkel, S. M. Vaiana, L. V. Bock, H. Grubmuller

The paper investigates how the ribosome exit tunnel drives the formation of a helical structure in the peptide VemP, leading to translational arrest.

bioRxiv · Apr 15, 2021Biophysics