title: The unfolding effects on the protein hydration shell and partial molar volume: a computational study.
abstract: In this paper we apply the computational analysis recently proposed by our group to characterize the solvation properties of a native protein in aqueous solution, and to four model aqueous solutions of globular proteins in their unfolded states thus characterizing the protein unfolded state hydration shell and quantitatively evaluating the protein unfolded state partial molar volumes. Moreover, by using both the native and unfolded protein partial molar volumes, we obtain the corresponding variations (unfolding partial molar volumes) to be compared with the available experimental estimates. We also reconstruct the temperature and pressure dependence of the unfolding partial molar volume of Myoglobin dissecting the structural and hydration effects involved in the process.
authors.affiliation: Department of Chemical Science and Technology, University of Roma Tor Vergata, via della Ricerca Scientifica, 00133 Roma, Italy. andrea.amadei@uniroma2.it.
authors.forename: Sara
authors.initials: S
authors.lastname: Del Galdo
authors.affiliation: Department of Chemical Science and Technology, University of Roma Tor Vergata, via della Ricerca Scientifica, 00133 Roma, Italy. andrea.amadei@uniroma2.it.
authors.forename: Andrea
authors.initials: A
authors.lastname: Amadei
mesh_terms: D009211:Myoglobin / Q000737:chemistry; D011312:Pressure; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature
chemical_list: D009211:Myoglobin