title: Crowding induces differences in the diffusion of thermophilic and mesophilic proteins: a new look at neutron scattering results.
abstract: The dynamical basis underlying the increased thermal stability of thermophilic proteins remains uncertain. Here, we challenge the new paradigm established by neutron scattering experiments in solution, in which the adaptation of thermophilic proteins to high temperatures lies in the lower sensitivity of their flexibility to temperature changes. By means of a combination of molecular dynamics and Brownian dynamics simulations, we report a reinterpretation of those experiments and show evidence that under crowding conditions, such as in vivo, thermophilic and homolog mesophilic proteins have diffusional properties with different thermal behavior.
authors.affiliation: Department of Biological Chemistry and Molecular Modeling, Institute of Advanced Chemistry of Catalonia (IQAC - CSIC), Barcelona, Spain.
authors.forename: Enrique
authors.initials: E
authors.lastname: Marcos
authors.forename: Pau
authors.initials: P
authors.lastname: Mestres
authors.forename: Ramon
authors.initials: R
authors.lastname: Crehuet
mesh_terms: D000818:Animals; D003198:Computer Simulation; D004058:Diffusion; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D046911:Macromolecular Substances / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D017017:Methanococcus / Q000201:enzymology*; D008958:Models, Molecular; D033363:Neutron Diffraction; D011817:Rabbits; D053838:Scattering, Small Angle; D055672:Static Electricity; D013696:Temperature
chemical_list: D046911:Macromolecular Substances; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase