Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile
Articles by Gregory L. Dignon
Hydration free energy is a significant predictor of globular protein incorporation into condensates
Abstract Membraneless organelles (MLOs) are assemblies of biomolecules, which function without a dividing lipid membrane in a cellular environment. These MLOs, termed biomolecular condensates, are commonly formed by the thermodynamic process of liquid-liquid phase separation (LLPS) and assembly of large numbers of proteins, nucleic acids and co-solvent molecules.
A computational procedure for predicting excipient effects on protein-protein affinities
Abstract Protein-protein interactions lie at the center of much biology and are a challenge in formulating biological drugs such as antibodies. A key to mitigating protein association is to use small molecule additives, i.e. excipients that can weaken protein-protein interactions.
Computational Procedure for Predicting Excipient Effects on Protein-Protein Affinities
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Chem. Theory Comput. 2024, XXXX, XXX Terms & Conditions Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses).
A coarse-grained model for position-specific effects of post-translational modifications on disordered protein phase separation
Abstract Biomolecules undergo liquid-liquid phase separation (LLPS) resulting in the formation of multicomponent protein-RNA membraneless organelles in cells. However, the physiological and pathological role of post translational modifications (PTMs) on the biophysics of phase behavior is only beginning to be probed.
Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior
Two ancient asteroids with distinctive diamond-like shapes are revealing clues not only about their own formation, but that of the solar system as well.
TDP-43 α-helical structure tunes liquid-liquid phase separation and function
TDP-43 α-helical structure tunes liquid–liquid phase separation and function Alexander E. Conicella, Gregory L. Dignon, Gül H. Zerze, Hermann Broder Schmidt, Alexandra M. D’Ordine, Young C. Kim, Rajat Rohatgi, Yuna M. Ayala, Jeetain Mittal, Nicolas L. Fawzi Proceedings of the National Academy of Sciences Mar 2020, 201912055; DOI: 10.1073/pnas.1912055117
Molecular interactions underlying liquid−liquid phase separation of the FUS low-complexity domain
Abstract The low-complexity domain of the RNA-binding protein FUS (FUS LC) mediates liquid−liquid phase separation (LLPS), but the interactions between the repetitive SYGQ-rich sequence of FUS LC that stabilize the liquid phase are not known in detail. By combining NMR and Raman spectroscopy, mutagenesis, and molecular simulation, we demonstrate that heterogeneous interactions involving all residue types underlie LLPS of human FUS LC.
Sequence determinants of protein phase behavior from a coarse-grained model
Loading metrics Open Access Peer-reviewed Research Article Gregory L. Dignon , Wenwei Zheng , Young C. Kim, Robert B. Best, Jeetain Mittal Gregory L. Dignon, Wenwei Zheng, Young C. Kim, Robert B.
Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation
hnRNPA2, a component of RNA-processing membraneless organelles, forms inclusions when mutated in a syndrome characterized by the degeneration of neurons (bearing features of amyotrophic lateral sclerosis [ALS] and frontotemporal dementia), muscle, and bone. Here we provide a unified structural view of hnRNPA2 self-assembly, aggregation, and interaction and the distinct effects of small chemical changes—disease mutations and arginine methylation—on these assemblies.
Show More
loading
Actions
Is this you?
As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.Get in touch with Gregory L.
Contact Gregory L., search articles and posts on X, monitor coverage, and track replies from one place.
Learn more about Muck Rack