News From The BARBAR LAB

Awards

2024 Gilfillian Award

Dr. Elisar Barbar was recognized as the College of Science 2024 Gilfillan award winner! The Gilfillan award recognizes distinguished scholarship in science by honoring a faculty member in the College of Science whose scholarship and scientific accomplishments have extended over a substantial period of time. On March 12, 2025, Barbar gave a lecture in which she reflected on the state of the field when she established her lab, reminisced about the discoveries she had made using interdisciplinary research, and explained how they changed the direction of the field.

Click HERE to watch the Gilfillian lecture.

Click HERE to read the full article.

2025 Inclusive Excellence Award

Hannah (graduate student in the Barbar Lab) was awarded the College of Science Inclusive Excellence Award for 2025. This award recognizes the outstanding work of a faculty, staff, or student in advancing inclusive excellence at OSU. Examples include helping to recruit students or employees from underrepresented communities to OSU, generating resources to advance EJI at OSU, promoting and advancing EJI at OSU, improving the climate of a unit within COS, supporting and advancing the cultural resource centers, advancing the role of women in science, or outstanding service as a search advocate. The award recognizes work primarily done at or for OSU, including contributions outside of COS.

Events

Sounds of Biophysics

As BPS student chapter president, Hannah organized the Sounds of Biophysics event in recognition of Biophysics Week. On April 4th the event featured seminars from Martin Gruebele of University of Illinois Urbana titled 'Sonification in biophysics for learning, research and data analysis' and Sarah Clark titled 'How we Hear.' There was also a live audio-visual musical performance by artist Jay A. Baker of a piece inspired by protein folding.

Publications

"Successful prediction of LC8 binding to intrinsically disordered proteins sheds light on AlphaFold’s black box"

Postdoc Douglas Walker envisioned and led a recent study, in collaboration with undergraduate researcher Gretchen Fujimura, to uncover how confidence information embedded in AlphaFold structure predictions can be used to accurately distinguish proteins that bind to the hub protein LC8 from those that do not. As Walker explains, “[The] structures are the superficial part of the prediction, and AlphaFold’s confidence in its own predictions must also be considered.”

In the process, the authors make a compelling case that AlphaFold has implicitly learned an energy function during training—one that, while not identical to the true protein folding energy landscape, is nevertheless informative. As statistician George Box famously put it, “All models are wrong, but some are useful.”

This work, guided by Elisar Barbar and Juan Vanegas, opens new avenues for understanding LC8 binding specificity and motif preference, while also providing insight into the inner workings of AlphaFold. The study is in print in Frontiers in Molecular Biosciences.

Walker, D. R., Fujimura, G., Vanegas, J. M., & Barbar, E. J. (2025). Successful prediction of LC8 binding to intrinsically disordered proteins sheds light on AlphaFold’s black box. Frontiers in Molecular Biosciences, 12, 1531793. https://doi.org/10.3389/fmolb.2025.1531793

Click HERE to read the article.

"Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: A comparative analysis of 14-3-3 and LC8"

Jesse Howe, a recent graduate from the Barbar lab, reviews the cellular functions, structures, and interactions of two well-characterized dimeric hub proteins, 14-3-3 and LC8. 14-3-3 is a dimeric phosphoserine/threonine binding protein with over 300 known clients involved in various cellular pathways. LC8 is a dimeric protein that functions in a number of biological processes, binding over 100 clients and promoting their dimerization. While both 14-3-3 and LC8 interact bivalently and share some conserved functions, such as in viral hijacking, their different structures and binding stoichiometries and mechanisms explain why 14-3-3 is primarily involved in regulation of phosphorylation states while LC8 is primarily involved in regulation of assembly of large dynamic complexes.

Howe J, Barbar EJ (2025) Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: a comparative analysis of 14-3-3 and LC8. J Biol Chem. https://doi.org/10.1016/j.jbc.2025.108416

Click HERE to read the article

"The BPTI Story: From the Slow Exchange Core to Intrinsically Disordered Proteins"

This is a review of the work on protein folding using BPTI as a model and the impact of these studies on the new field of intrinsically disordered proteins. This review is part of the issue celebrating the retirement of Professor George Barany, Dr. Barbar's postdoctoral co-advisor who, alongside Clare Woodward, made significant contributions to peptide chemistry and biophysics. Their work led to new discoveries in protein folding and the field of intrinsically disordered proteins.

Barbar, E.J. The BPTI Story: From the Slow Exchange Core to Intrinsically Disordered Proteins. Int J Pept Res Ther 31, 55 (2025). https://doi.org/10.1007/s10989-025-10714-1

Click HERE to read the article.

Instrumentation

New ITC

Recently, the Barbar lab has acquired a brand-new ITC machine. Isothermal Titration Calorimetry (ITC) is a method that measures changes in heat of binding events to determine the thermodynamic characteristics. This new machine is significantly more sensitive than the other, allowing for runs with much less substrate required while obtaining similar results. They also have some new data analyzing software that allows users to quickly understand data trends and thermodynamic characteristics. To get the best results, make sure to add an extra 50 microliters to the injection syringe to avoid problems with dead volume, and always degas your samples!