Modulation in the Structure, Dynamics, and Enzymatic Activity of an Ordered Protein β-Lactoglobulin through Liquid-Liquid Phase Separation

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dc.contributor.authorMukherjee ,Saptarshi
dc.date.accessioned2025-07-14T09:34:39Z
dc.date.available2025-07-14T09:34:39Z
dc.date.issued2025-05
dc.descriptionT heme Seminar Page 25
dc.description.abstractBimolecular condensates formed through liquid–liquid phase separation (LLPS) of proteins, polypeptides, and nucleic acids have garnered significant research of late.1-3 Despite valuable contributions of prior research, there is untapped potential in exploring the influence of phase separation on the conformational dynamics and enzymatic activities of native proteins.
dc.identifier.urihttps://dr.ichemc.ac.lk/handle/123456789/413
dc.language.isoen
dc.publisherInstitute of Chemistry Ceylon
dc.relation.ispartofseries42; 2
dc.subjectStructure
dc.subjectDynamics
dc.subjectand Enzymatic Activity
dc.subjectLiquid Phase Separation
dc.titleModulation in the Structure, Dynamics, and Enzymatic Activity of an Ordered Protein β-Lactoglobulin through Liquid-Liquid Phase Separation
dc.typeArticle

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