A
Archishman Ghosh
Researcher at University of Illinois at Chicago
Publications - 10
Citations - 178
Archishman Ghosh is an academic researcher from University of Illinois at Chicago. The author has contributed to research in topics: Viscoelasticity & Shear stress. The author has an hindex of 4, co-authored 9 publications receiving 94 citations. Previous affiliations of Archishman Ghosh include Florida State University.
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Three archetypical classes of macromolecular regulators of protein liquid–liquid phase separation
TL;DR: By measuring the effects on the phase boundary and the levels of partitioning into the condensates of 2 proteins (SH35 and PRM5), 3 archetypical classes of macromolecular regulators are defined, providing a much needed understanding of the regulatory effects of membraneless organelles.
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Shear relaxation governs fusion dynamics of biomolecular condensates
TL;DR: In this article, the authors used optically trapped polystyrene beads to measure the viscous and elastic moduli and the interfacial tensions of four types of droplets, and reveal that the relaxation of shear stress governs fusion dynamics.
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Determinants for Fusion Speed of Biomolecular Droplets.
Archishman Ghosh,Huan-Xiang Zhou +1 more
TL;DR: Using a dual-trap optical tweezers setup, the fusion speeds of four types of droplets to differ by two orders of magnitude are found, and a molecular interpretation for disparate fusion speeds provides mechanistic insight into the assembly and aging of biomolecular droplets.
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Tug of War between Condensate Phases in a Minimal Macromolecular System.
TL;DR: In this paper, the authors demonstrate a range of phase behaviors associated with membraneless organelles and uncover the underlying physicochemical rules, including rescue of aberrant phase transitions, demixing of condensates, and time evolution of material properties.
Journal ArticleDOI
Both Ligands and Macromolecular Crowders Preferentially Bind to Closed Conformations of Maltose Binding Protein.
Archishman Ghosh,Archishman Ghosh,Pieter E. S. Smith,Sanbo Qin,Sanbo Qin,Myunggi Yi,Huan-Xiang Zhou,Huan-Xiang Zhou +7 more
TL;DR: Conformational and site preferences in MBP-crowder binding allude to the paradigm that nonspecific interactions can possess hallmarks of molecular recognition, which may be essential for intracellular organizations including colocalization of proteins and liquid-liquid phase separation.