Understanding intrinsically disordered protein regions and their roles in cancer

Every function in a cell is associated with a particular protein or group of proteins, typically in a well-defined three-dimensional structure. However, intrinsically disordered regions of proteins defy this structure-function paradigm. A team of researchers in the McKelvey School of Engineering at Washington University in St. Louis has developed an algorithm to understand how intrinsically […]

WashU chemists reveal new insights into ALS-linked protein

Using advanced techniques in biophysical chemistry, a team led by Meredith Jackrel, PhD, an associate professor of chemistry, has achieved unprecedented views of a protein that may play a pivotal role in some cases of amyotrophic lateral sclerosis (ALS) and the related disorder frontotemporal dementia (FTD). Their work could open doors to new approaches for treatment […]

Research untangles role of stress granules in neurodegenerative disease

Scientists from St. Jude Children’s Research Hospital and Washington University in St. Louis report mechanistic insights into the role of biomolecular condensation in the development of neurodegenerative disease. The collaborative research, published in Molecular Cell, focused on the interactions that drive the formation of condensates versus the formation of amyloid fibrils and how these relate to […]

Myosin makes the moves to keep cell processes humming along

Biomolecular condensates are distinct molecular communities made of DNA, RNA and proteins that “condense” molecules to key locations inside cells. Intense efforts have focused on uncovering the numerous ways in which condensation is controlled, modulated and regulated inside cells. In research published May 23 in Science Advances, biomedical scientists at Washington University in St. Louis and […]

A closer look at biomolecular ‘Silly Putty’

Biomolecular condensates are shifting blobs in our cells that organize cellular matter. They are distinct molecular communities made of DNA, RNA and proteins that “condense” molecules to key locations, yet they frequently defy description. Partly this is because they are so small, they cannot be measured using traditional microscopes. “These blobs were once described as […]

2025 Olin Fellows & Kipnis Awardees

On behalf of the Medical Scientist Training Program Committee, we are pleased to announce the recipients of this year’s Spencer T. and Ann W. Olin Medical Science Fellows: The Olin Fellowships recognize superior accomplishments in biomedical research by doctoral students at Washington University. 32 outstanding students were nominated for the Olin Fellows Award this year, […]

Pappu named American Physical Society fellow

Rohit V. Pappu, PhD, the Gene K. Beare Distinguished Professor of Biomedical Engineering and director of the Center for Biomolecular Condensates at Washington University in St. Louis, has been selected as an American Physical Society Fellow. Pappu was selected for his innovative and fundamental studies regarding intrinsically disordered proteins and phase transitioning behaviors using polymer […]

WashU engineers manage a first: measuring pH in cell condensates

Scientists trying to understand the physical and chemical properties that govern biomolecular condensates now have a crucial way to measure pH and other emergent properties of these enigmatic, albeit important cellular compartments. Condensates are communities of proteins and nucleic acids. They lack a membrane and come together and fall apart as needed. The nucleolus is […]

Pappu installed as Gene K. Beare Distinguished Professor of Biomedical Engineering

Rohit V. Pappu, PhD, an internationally renowned researcher in biomolecular condensates and intrinsically disordered proteins, was installed Oct. 9 as the Gene K. Beare Distinguished Professor of Biomedical Engineering at Washington University in St. Louis. Pappu is a professor of biomedical engineering and director of the Center for Biomolecular Condensates at the McKelvey School of […]

Pappu to explore ways in which charge contributes to diverse states of proteins

Intrinsically disordered proteins (IDPs) are defined by structural diversity, and the determinants of this diversity are an important area of biophysical investigation. IDPs are involved in a range of important biological processes, including cell signaling and regulation, that allow healthy cells to respond to environmental factors appropriately, but they are also associated with human diseases […]

How do cells take out the trash?

Research uncovers how unfolded proteins are discarded, and how a perfectly good protein can wind up in the trash

New structure found in cells

Every cell contains millions of protein molecules. Some of them have the ability to phase-separate to form non-membrane-bound compartments, called biomolecular condensates, inside a cell. It has long been assumed that there was no further structure underlying these condensates, only solution-soluble proteins. A research group led by Rohit Pappu, PhD, the Gene K. Beare Distinguished Professor […]

Pappu lab untangles more IDR secrets

Intrinsically disordered regions (IDRs) of proteins, when tethered to folded domains, function either as flexible tails or as linkers between domains. Most IDRs are composed of a mixture of oppositely charged residues. Recent measurements of tethered polyampholytes have shown that arginine- and lysine-rich sequences tend to behave very differently from one another. In a paper […]