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Paolo Calligari

Researcher at University of Rome Tor Vergata

Publications -  32
Citations -  688

Paolo Calligari is an academic researcher from University of Rome Tor Vergata. The author has contributed to research in topics: Allosteric regulation & Proto-oncogene tyrosine-protein kinase Src. The author has an hindex of 12, co-authored 31 publications receiving 491 citations. Previous affiliations of Paolo Calligari include International School for Advanced Studies & École Normale Supérieure.

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Simulation studies of structural changes and relaxation processes in lysozyme under pressure

TL;DR: In this article, preliminary results of a molecular dynamics simulation study on the influence of non-denaturing hydrostatic pressure on the structure and the relaxation dynamics of lysozyme were presented.
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Multiple scale dynamics in proteins probed at multiple time scales through fluctuations of NMR chemical shifts.

TL;DR: The proposed fractional diffusion model may provide significative improvement to the analysis of NMR dispersion experiments and the predicted exchange contribution Rex to the NMR transverse relaxation rate is in qualitative agreement with experimental results.
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Toward the Characterization of Fractional Stochastic Processes Underlying Methyl Dynamics in Proteins

TL;DR: This analysis highlights the presence of the asymptotic power law decay of the waiting time probability density of the stochastic process involved, thereby illustrating the connection between approaches based on fractional diffusion equations and the continuous time random walk.
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Communication: a minimal model for the diffusion-relaxation backbone dynamics of proteins.

TL;DR: It is demonstrated that the model fits the position autocorrelation functions of the C(α)-atoms exceptionally well and reveals moreover a strong correlation between the residue's solvent-accessible surface and the fitted model parameters.
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Targeting the Pentose Phosphate Pathway: Characterization of a New 6PGL Inhibitor.

TL;DR: This work has focused on the activity of the second PPP enzyme (6-phospho-gluconolactonase (6PGL) that transforms 6- phosphoglu Conolactone into 6-ph phosphogluconic acid, and demonstrated a marginal inhibition of the third enzyme of the PPP (6 -phosphogluconate dehydrogenase) that was demonstrated.