ACS Biophysical Subdivision

The Biophysical Subdivision of the PHYS technical division serves the biophysical chemistry community of ACS. Founded in 1995, the subdivision represents a broad spectrum of biophysics research topics, with a common theme of applying physical chemistry measurement and modeling approaches to tackle biological questions at the molecular and supramolecular levels. Its goal is to present new biophysics research as part of PHYS programming at national meetings and connect a diverse group of scientists and educators who are passionate about biophysical chemistry.

Current officers:

Chair: Lydia Kisley, Case Western Reserve University
(216) 368-2118,

Chair-Elect: Itay Budin, UC-San Diego
(858) 246-5328,

Vice-Chair: Colin Heyes, University of Arkansas
(479) 575-5607,

Past chairs (current affiliation and ending year of their term as chair):

Galia Debelouchina (UCSD, 2023), Carlos Baiz (UT Austin, 2022), Renee Frontiera (UMN, 2021), Julie Biteen (Michigan, 2020), Casey Londergan (Haverford, 2019), Christy Landes (UIUC, 2018), Qiang Cui (Boston, 2017), Lauren Webb (UT Austin, 2016), Kimberly Hamad-Schifferli (U Mass Boston, 2015), Steve Corcelli (Notre Dame, 2014), Judy Kim, (2013), Greg Engel (Chicago, 2012), Doug Tobias (UC Irvine, 2011), Christine Payne (Duke, 2010), Martin Zanni (Wisconsin, 2009), Cecilia Clementi (Free University Berlin, 2008), Jeffrey Saven (Penn, 2007), Jay R. Winkler (Caltech, 2006), Benoit Roux (Chicago, 2005), Zaida Luthey-Schulten (UIUC, 2004), Peter G. Wolynes (Rice, 2003), Arieh Warshel (USC, 2002), William A. Eaton (NIH, 2001), Eric Oldfield (UIUC, 2000), Robin M. Hochstrasser (Penn, 1999), Robert G. Griffin (MIT, 1998), Graham R. Fleming (UC Berkeley, 1997), Richard Mathies (UC Berkeley, 1996)

How to join:

Are you not an ACS member yet? You can join the American Chemical Society, the Physical Chemistry Division, and the Biophysical Subdivision when becoming a member.

Are you already an ACS member? Use your ACS membership to join the Physical Chemistry Division and the Biophysical Subdivision.

Are you already an ACS PHYS member? Email ACS Member Services at indicating your desire to join the Biophysical Subdivision.

Propose a future biophysical chemistry symposium for an ACS National Meeting!  

Please email the current chair with a title and brief one paragraph summary of your symposium topic. The chair will then follow up with information if a full proposal is requested. A full proposal requires a summary, a tentative list of diverse invited speakers, and proposed fundraising opportunities. Realize that slots are limited and an initial inquiry for a symposium should be submitted ~2 years in advance of the desired conference.

Upcoming symposia: 

2025 Fall Meeting Denver:

Elucidating the Chemical Specificity of Biomolecular Condensates (Organized by Rosana Collepardo, Galia Debelouchina, Bin Zhang) Biological condensates play essential roles in various cellular processes, from stress response to genome organization. Similar to membrane-bound organelles, they assemble a collection of molecules to raise the efficiency of sophisticated tasks. The lack of a membrane barrier allows fast material exchange between condensates and the cellular environment, rendering the molecular composition and stability of condensates more prone to regulations by external signals. Intrinsically disordered proteins (IDPs) that promote multivalent, promiscuous interactions are key drivers of condensate formation. Multiple mechanisms, including electrostatic, cation-π, hydrogen bonding, and hydrophobic interactions, contribute to the affinity among various chemical groups. Above a threshold concentration, as predicted by the Flory-Huggins theory, interactions among IDPs can drive liquid-liquid phase separation to produce a highly concentrated phase that nevertheless remains dynamic. Despite significant progress, much remains to be learned regarding the connection between amino acid sequences and protein phase behaviors, or the so-called “molecular grammar” of protein condensates. Systematic and quantitative structural and chemical characterizations of condensates are necessary to understand their organizational principles further. This symposium will bring together theorists and experimentalists to present the latest progress in studying biomolecular condensates, identify future challenges, and promote collaboration

Understanding Protein Structure with Spatially and Temporally Resolved Spectroscopy (Organized by Nancy Levinger, Jyotishman Dasgupta) At the heart of many fundamental biological and pathological processes is the transformation and evolution of specific structures by protein and peptide assemblies. A persistent experimental challenge is the development of biophysical approaches that offer new insights into protein conformation and dynamics. Application of ultrafast time-resolved spectroscopies has led to successful experimental designs that leverage the nonlinearity of protein signals and provide site-specific structural constraints, akin to nuclear magnetic resonance spectroscopy. More recent advances have augmented molecular spectroscopies with spatially-resolved imaging techniques, revealing individual structures within an ensemble. The advent of cryoelectron microscopy has furthered the potential of spatially-resolved structural mapping of biomolecular self-assemblies. Altogether, these approaches probe protein structure with unprecedented detail. This symposium will bring together experts in imaging, spectroscopic, and computational methods, and we encourage invited speakers to frame their talks with respect to recent advances and future challenges for the field, in the hopes of spurring conversations and collaborations that will advance our understanding of how protein structures evolve related to both biological function and pathological consequences

Example of past symposia:

Please refer to the PHYS archives “Call for Papers” for full listings of symposia at

Optical Spectroscopy and Microscopy Across Biological Scales (organized by Gabriela Schlau-Cohen and Lu Wei): Optical spectroscopy and microscopy have allowed investigations of the complex biological structures and dynamics across different scales with unprecedented precision in space, time, and function. This symposium will bring together experimentalists and theorists with various spectroscopic and microscopic specialties ranging from nonlinear spectroscopy to single-molecule spectroscopy; from fluorescence imaging to Raman/IR or other label-free modalities; from fundamental biophysics on protein dynamics to investigations on the live cell, neuron and animal levels; and across different career stages to discuss the recent technical and application advances and brainstorm key issues and questions.

Frontiers of Structural Biology in Complex Environments (organized by Matthew Eddy, Kendra Frederick, Dylan T. Murray): Decades of careful experimentation and analysis by biophysical chemists have formed a foundation for contemporary scientists to understand the structure and function of proteins in the incredibly complex environments of living organisms. Recent advances in experimental and computational approaches have made it possible to describe and predict the structure, dynamics, and interactions of biomolecular assemblies in complex environments in vitro, in situ, in cells, and in the extracellular environment. Despite these exciting advances, many challenges remain in integrating techniques and approaches that span multiple time and length scales, and in understanding how atomic level changes drive functional biological outputs in the cellular environment. The symposium will bring together experimentalists and theorists who apply cutting-edge methods to determine the structure of biomolecules at or near atomic level precision in such environments. Speakers will discuss recent progress in the field and future challenges in the areas (1) atomic resolution studies of large complexes, (2) biomolecular condensation, (3) in situ studies in cell and cell-like environments, (4) in vitro cellular environments, and (5) biophysical experiments in multi-cellular environments.

The Physical Chemistry of Co-translational Protein Folding (organized by Stephen D. Fried, Silvia Cavagnero, Edward O’Brien): Protein folding has long been interpreted through the lens of in vitro refolding experiments on small proteins that conform to two-(or few) state models, though this may be a poor model for how proteins fold in the cell, which occurs cotranslationally on the ribosome. Translation makes folding an inherently kinetic phenomenon replete with irreversible steps, and may be required for the folding of more complex ‘non-model’ proteins. This symposium will critically elucidate differences between protein folding in vivo compared to traditional in vitro refolding assays so as to shed light as to where our ‘received truths’ about protein folding might need to be reconsidered. It will also emphasize the important interplay between computation and novel experimental techniques to elucidate a complex process that is somewhat elusive to traditional methods in biophysical chemistry and structural biology.