Biophysical Society Bulletin | February 2026

Publications

Know the Editor Alexandra Zidovska New York University

Editor’s Pick

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Editor, Genome Biophysics and Nucleic Acids Biophysical Journal

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Alexandra Zidovska

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What are you currently working on that excites you? I am very excited by trying to understand physical principles underlying the organization and dynamics of the human genome. The genome is endlessly complex and intricately organized inside the cell nucleus. Really, 2 m of DNA are packed inside a cell nucleus barely 10 µm in diameter, so the cell has to use nifty tricks to do so, and many of them rely on physics. On top of it, it’s not only a packing problem, it also has to be packed in a way that allows easy and fast access to different parts of the genome. Like a gigantic library with easy access to any book you want. At the same time, the genome is dynamic, so this question has literally and figuratively many moving parts. What has been your most exciting discovery as a biophysicist? My most exciting discovery has been the discovery of coher ent motions of the genome in live cells. Using displacement correlation spectroscopy (DCS), I found that big patches of chromatin—the functional form of DNA in the cell—are moving together for several seconds inside the cell nucleus. This type of motion is present in the cell only when active processes, which use ATP as fuel, are ongoing. Without ATP, it is gone. The coherent chromatin motions are a very inter esting phenomenon, as they cause a group of genes to travel together for a short time, and clearly affect the genome organization in the cell nucleus. This is interesting from both a physics and a biology perspective, because it informs our current picture of the genome.

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Biophysical Journal Backbone conformational entropy change in helix folding Uroš Zavrtanik, Jurij Lah, and San Hadži “One aspect of the protein folding problem concerns the question of what makes proteins thermodynamically stable. It is known that stability results from a delicate balance among several thermodynamic forces, of which the largest oppos ing folding arises from the loss of conformational freedom, reflected in the backbone entropy change, ΔS BB . However, the value of this key parameter is difficult to determine exper imentally. By measuring the absolute heat capacity of the simplest protein folding unit, the α -helix, and using a sta tistical-thermodynamic model and Bayesian inference, the authors determined the helix nucleation parameter that is directly related to ΔS BB . The resulting precise ΔS BB value is cru cial for a better understanding of how thermodynamic driving forces orchestrate protein stability.”

Version of Record Published November 28, 2025 DOI: https:/doi.org/10.1016/j.bpj.2025.11.2689

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The Biophysical Society has a global membership, with approximately one-third of our members located outside the United States.

February 2026

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