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340 results on '"Temussi, PIERO ANDREA"'

7. Revitalizing an important field in biophysics: The new frontiers of molecular crowding

Author

European Commission, Cammarata, Marco [0000-0003-3013-1186], Piazza, Francesco [0000-0003-0205-3790], Rivas, Germán [0000-0003-3450-7478], Schirò, Giorgio [0000-0002-8113-4937], Temussi, Piero Andrea [0000-0001-6032-4291], Pastore, Annalisa [0000-0002-3047-654X], Cammarata, Marco, Piazza, Francesco, Rivas, Germán, Schirò, Giorgio, Temussi, Piero Andrea, Pastore, Annalisa, European Commission, Cammarata, Marco [0000-0003-3013-1186], Piazza, Francesco [0000-0003-0205-3790], Rivas, Germán [0000-0003-3450-7478], Schirò, Giorgio [0000-0002-8113-4937], Temussi, Piero Andrea [0000-0001-6032-4291], Pastore, Annalisa [0000-0002-3047-654X], Cammarata, Marco, Piazza, Francesco, Rivas, Germán, Schirò, Giorgio, Temussi, Piero Andrea, and Pastore, Annalisa

Abstract

Taking into account the presence of the crowded environment of a macromolecule has been an important goal of biology over the past 20 years. Molecular crowding affects the motions, stability and the kinetic behaviour of proteins. New powerful approaches have recently been developed to study molecular crowding, some of which make use of the synchrotron radiation light. The meeting “New Frontiers in Molecular Crowding” was organized in July 2022at the European Synchrotron Radiation facility of Grenoble to discuss the new frontiers of molecular crowding. The workshop brought together researchers from different disciplines to highlight the new developments of the field, including areas where new techniques allow the scientists to gain unprecedently expected information. A key conclusion of the meeting was the need to build an international and interdisciplinary research community through enhanced communication, resource-sharing, and educational initiatives that could let the molecular crowding field flourish further.

Published
2023

49. A natural and readily available crowding agent: NMR studies of proteins in hen egg white

Author

Martorell Gabriel, Adrover Miquel, Kelly Geoff, Temussi Piero Andrea, Pastore A, Martorell, Gabriel, Adrover, Miquel, Kelly, Geoff, Temussi Piero, Andrea, and Pastore, A

Subjects
folding, Egg White, Protein Stability, confinement, aggregation, cytoplasm, Temperature, Animals, Proteins, stability, Chickens, Nuclear Magnetic Resonance, Biomolecular, Research Article
Abstract

In vitro studies of biological macromolecules are usually performed in dilute, buffered solutions containing one or just a few different biological macromolecules. Under these conditions, the interactions among molecules are diffusion limited. On the contrary, in living systems, macromolecules of a given type are surrounded by many others, at very high total concentrations. In the last few years, there has been an increasing effort to study biological macromolecules directly in natural crowded environments, as in intact bacterial cells or by mimicking natural crowding by adding proteins, polysaccharides, or even synthetic polymers. Here, we propose the use of hen egg white (HEW) as a simple natural medium, with all features of the media of crowded cells, that could be used by any researcher without difficulty and inexpensively. We present a study of the stability and dynamics behavior of model proteins in HEW, chosen as a prototypical, readily accessible natural medium that can mimic cytosol. We show that two typical globular proteins, dissolved in HEW, give NMR spectra very similar to those obtained in dilute buffers, although dynamic parameters are clearly affected by the crowded medium. The thermal stability of one of these proteins, measured in a range comprising both heat and cold denaturation, is also similar to that in buffer. Our data open new possibilities to the study of proteins in natural crowded media. Proteins 2011. © 2010 Wiley-Liss, Inc.

Published
2010

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