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Full-Text Articles in Medicine and Health Sciences
Liaisons Dangereuses: Intrinsic Disorder In Cellular Proteins Recruited To Viral Infection-Related Biocondensates, Greta Bianchi, Stefania Brocca, Sonia Longhi, Vladimir N. Uversky
Liaisons Dangereuses: Intrinsic Disorder In Cellular Proteins Recruited To Viral Infection-Related Biocondensates, Greta Bianchi, Stefania Brocca, Sonia Longhi, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Liquid–liquid phase separation (LLPS) is responsible for the formation of so-called membrane-less organelles (MLOs) that are essential for the spatio-temporal organization of the cell. Intrinsically disordered proteins (IDPs) or regions (IDRs), either alone or in conjunction with nucleic acids, are involved in the formation of these intracellular condensates. Notably, viruses exploit LLPS at their own benefit to form viral replication compartments. Beyond giving rise to biomolecular condensates, viral proteins are also known to partition into cellular MLOs, thus raising the question as to whether these cellular phase-separating proteins are drivers of LLPS or behave as clients/regulators. Here, we focus on …
Biapss: A Comprehensive Physicochemical Analyzer Of Proteins Undergoing Liquid–Liquid Phase Separation, Aleksandra E. Badaczewska-Dawid, Vladimir N. Uversky, Davit A. Potoyan
Biapss: A Comprehensive Physicochemical Analyzer Of Proteins Undergoing Liquid–Liquid Phase Separation, Aleksandra E. Badaczewska-Dawid, Vladimir N. Uversky, Davit A. Potoyan
Molecular Medicine Faculty Publications
The liquid–liquid phase separation (LLPS) of biomolecules is a phenomenon which is nowadays recognized as the driving force for the biogenesis of numerous functional membraneless organelles and cellular bodies. The interplay between the protein primary sequence and phase separation remains poorly understood, despite intensive research. To uncover the sequence-encoded signals of protein capable of undergoing LLPS, we developed a novel web platform named BIAPSS (Bioinformatics Analysis of LLPS Sequences). This web server provides on-the-fly analysis, visualization, and interpretation of the physicochemical and structural features for the superset of curated LLPS proteins.
Hydrogen Bond Arrangement Is Shown To Differ In Coexisting Phases Of Aqueous Two-Phase Systems, Pedro P. Madeira, Amber R. Titus, Luisa A. Ferreira, Alexander I. Belgovskiy, Elizabeth K. Mann, Jay Adin Mann Jr., William V. Meyer, Anthony E. Smart, Vladimir N. Uversky, Boris Zaslavsky
Hydrogen Bond Arrangement Is Shown To Differ In Coexisting Phases Of Aqueous Two-Phase Systems, Pedro P. Madeira, Amber R. Titus, Luisa A. Ferreira, Alexander I. Belgovskiy, Elizabeth K. Mann, Jay Adin Mann Jr., William V. Meyer, Anthony E. Smart, Vladimir N. Uversky, Boris Zaslavsky
Molecular Medicine Faculty Publications
Analysis by attenuated total reflection–Fourier transform infrared spectroscopy shows that each coexisting phase in aqueous two-phase systems has a different arrangement of hydrogen bonds. Specific arrangements vary for systems formed by different solutes. The hydrogen bond arrangement is shown to correlate with differences in hydrophobic and electrostatic properties of the different phases of five specific systems, four formed by two polymers and one by a single polymer and salt. The results presented here suggest that the arrangement of hydrogen bonds may be an important factor in phase separation.
Driving Forces Of Liquid–Liquid Phase Separation In Biological Systems, Boris Y. Zaslavsky, Luisa A. Ferreira, Vladimir N. Uversky
Driving Forces Of Liquid–Liquid Phase Separation In Biological Systems, Boris Y. Zaslavsky, Luisa A. Ferreira, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Analysis of liquid–liquid phase separation in biological systems shows that this process is similar to the phase separation observed in aqueous two-phase systems formed by nonionic polymers, proteins, and polysaccharides. The emergence of interfacial tension is a necessary condition of phase separation. The situation in this regard is similar to that of phase separation in mixtures of partially miscible solvents. It is suggested that the evaluation of the effects of biological macromolecules on the solvent properties of aqueous media and the measurement of the interfacial tension as a function of these solvent properties may be more productive for gaining insights …
Life In Phases: Intra- And Inter- Molecular Phase Transitions In Protein Solutions, Vladimir N. Uversky, Alexey V. Finkelstein
Life In Phases: Intra- And Inter- Molecular Phase Transitions In Protein Solutions, Vladimir N. Uversky, Alexey V. Finkelstein
Molecular Medicine Faculty Publications
Proteins, these evolutionarily-edited biological polymers, are able to undergo intramolecular and intermolecular phase transitions. Spontaneous intramolecular phase transitions define the folding of globular proteins, whereas binding-induced, intra- and inter- molecular phase transitions play a crucial role in the functionality of many intrinsically-disordered proteins. On the other hand, intermolecular phase transitions are the behind-the-scenes players in a diverse set of macrosystemic phenomena taking place in protein solutions, such as new phase nucleation in bulk, on the interface, and on the impurities, protein crystallization, protein aggregation, the formation of amyloid fibrils, and intermolecular liquid–liquid or liquid–gel phase transitions associated with the biogenesis …