Marc Antoine Ceruso

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The dynamics of collective protein motions derived from Molecular Dynamics simulations have been studied for two small model proteins: initiation factor I and the B1 domain of Protein G. First, we compared the structural fluctuations, obtained by local harmonic approximations in different energy minima, with the ones revealed by large scale molecular(More)
The analysis of the dynamic behavior of enzymes is fundamental to structural biology. A direct relationship between protein flexibility and biological function has been shown for bovine pancreatic ribonuclease (RNase A) (Rasmussen et al., Nature 1992;357:423-424). More recently, crystallographic studies have shown that functional motions in RNase A involve(More)
The understanding of protein dynamics is one of the major goals of structural biology. A direct link between protein dynamics and function has been provided by x-ray studies performed on ribonuclease A (RNase A) (B. F. Rasmussen et al., Nature, 1992, Vol. 357, pp. 423-424; L. Vitagliano et al., Proteins: Structure, Function, and Genetics, 2002, Vol. 46, pp.(More)
  • Cecilia Bossa, Relatore Alfredo Di, Nola, Docenti Esaminatori, bullet D Roccatano, I Daidone +19 others
  • 2005
excitation of native fluctuations during thermal unfolding simulations: horse heart cytochrome c, a case study. Biophys. Conformational fluctuations and electronic properties in myoglobin. A. Di Nola. Extended molecular dynamics simulation of the carbon monoxide migration in sperm whale myoglobin. Biophys. A. Di Nola. Molecular dynamics simulations of sperm(More)
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