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University of South Florida

Molecular Medicine Faculty Publications

2019

Protein Structure

Articles 1 - 2 of 2

Full-Text Articles in Medicine and Health Sciences

Life In Phases: Intra- And Inter- Molecular Phase Transitions In Protein Solutions, Vladimir N. Uversky, Alexey V. Finkelstein Jan 2019

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 …


Structure Determination By Single-Particle Cryo-Electron Microscopy: Only The Sky (And Intrinsic Disorder) Is The Limit, Emeka Nwanochie, Vladimir N. Uversky Jan 2019

Structure Determination By Single-Particle Cryo-Electron Microscopy: Only The Sky (And Intrinsic Disorder) Is The Limit, Emeka Nwanochie, Vladimir N. Uversky

Molecular Medicine Faculty Publications

Traditionally, X-ray crystallography and NMR spectroscopy represent major workhorses of structural biologists, with the lion share of protein structures reported in protein data bank (PDB) being generated by these powerful techniques. Despite their wide utilization in protein structure determination, these two techniques have logical limitations, with X-ray crystallography being unsuitable for the analysis of highly dynamic structures and with NMR spectroscopy being restricted to the analysis of relatively small proteins. In recent years, we have witnessed an explosive development of the techniques based on Cryo-electron microscopy (Cryo-EM) for structural characterization of biological molecules. In fact, single-particle Cryo-EM is a special …