alessandro Paciaroni

Prof. alessandro Paciaroni


Research Focus & Metrics

Academic Career Length

32Years (1995-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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3 March 2015 in JAMA
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Journal Article
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CDCosimo Durante
Cosimo Durante
GCGiuseppe Costante
Giuseppe Costante
GLGiuseppe Lucisano
Giuseppe Lucisano
RBRocco Bruno
Rocco Bruno
DMDomenico Meringolo
Domenico Meringolo
SFSebastiano Filetti
Sebastiano Filetti
Research from JAMA — The Natural History of Benign Thyroid Nodules

19 May 2016 in Chemical Reviews
Verified
Journal Article
Closed access
KAKatrin Amann-Winkel
Katrin Amann-Winkel
Marie-Claire Bellissent-FunelMarie-Claire Bellissent-Funel
Marie-Claire Bellissent-Funel
LBLivia Eleonora Bove
Livia Eleonora Bove
TLThomas Loerting
Thomas Loerting
ANAnders Nilsson
Anders Nilsson
LSLawrie Skinner
Lawrie Skinner

16 March 2015 in Nature Communications
Verified
Journal Article
Open access
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GSGiorgio Schirò
Giorgio Schirò
YFYann Fichou
Yann Fichou
FGFrancois-Xavier Gallat
Francois-Xavier Gallat
KWKathleen Wood
Kathleen Wood
FGFrank Gabel
Frank Gabel
MWMartin Weik
Martin Weik
Hydration water is the natural matrix of biological macromolecules and is essential for their activity in cells. The coupling between water and protein dynamics has been intensively studied, yet it remains controversial. Here we combine protein perdeuteration, neutron scattering and molecular dynamics simulations to explore the nature of hydration water motions at temperatures between 200 and 300 K, across the so-called protein dynamical transition, in the intrinsically disordered human protein tau and the globular maltose binding protein. Quasi-elastic broadening is fitted with a model of translating, rotating and immobile water molecules. In both experiment and simulation, the translational component markedly increases at the protein dynamical transition (around 240 K), regardless of whether the protein is intrinsically disordered or folded. Thus, we generalize the notion that the translational diffusion of water molecules on a protein surface promotes the large-amplitude motions of proteins that are required for their biological activity.

14 March 2008 in Journal of the American Chemical Society
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Journal Article
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KWKathleen Wood
Kathleen Wood
AFAndreas Frölich
Andreas Frölich
APalessandro Paciaroni
alessandro Paciaroni
MMMartine Moulin
Martine Moulin
MHMichael Härtlein
Michael Härtlein
MWMartin Weik
Martin Weik

1 August 2002 in Biophysical Journal
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Journal Article
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APalessandro Paciaroni
alessandro Paciaroni
SCStefania Cinelli
Stefania Cinelli
GOGiuseppe Onori
Giuseppe Onori

1 July 2009 in Journal of The Royal Society Interface
Verified
Journal Article
Closed access
Maria Grazia OrtoreMaria Grazia Ortore
Maria Grazia Ortore
FSFrancesco Spinozzi
Francesco Spinozzi
Paolo MarianiPaolo Mariani
Paolo Mariani
APalessandro Paciaroni
alessandro Paciaroni
LBLeandro R. S. Barbosa
Leandro R. S. Barbosa
DRDaniela Russo
Daniela Russo
Small-angle X-ray scattering (SAXS) and elastic and quasi-elastic neutron scattering techniques were used to investigate the high-pressure-induced changes on interactions, the low-resolution structure and the dynamics of lysozyme in solution. SAXS data, analysed using a global-fit procedure based on a new approach for hydrated protein form factor description, indicate that lysozyme completely maintains its globular structure up to 1500 bar, but significant modifications in the protein–protein interaction potential occur at approximately 600–1000 bar. Moreover, the mass density of the protein hydration water shows a clear discontinuity within this pressure range. Neutron scattering experiments indicate that the global and the local lysozyme dynamics change at a similar threshold pressure. A clear evolution of the internal protein dynamics from diffusing to more localized motions has also been probed. Protein structure and dynamics results have then been discussed in the context of protein–water interface and hydration water dynamics. According to SAXS results, the new configuration of water in the first hydration layer induced by pressure is suggested to be at the origin of the observed local mobility changes.