Essential dynamics of the cold denaturation: pressure and temperature effects in yeast frataxin.
The cold denaturation of globular proteins is a process that can be caused by increasing pressure or decreasing the temperature. Currently, the action mechanism of this process has not been clearly understood, raising an interesting debate on the matter. We have studied the process of cold denaturation using molecular dynamics simulations of the frataxin system Yfh1, which has a dynamic experimental characterization of unfolding at low and high temperatures. The frataxin model here studied allows a comparative analysis using experimental data. Furthermore, we monitored the cold denaturation process of frataxin and also investigated the effect under the high-pressure regime. For a better understanding of the dynamics and structural properties of the cold denaturation, we also analyzed the MD trajectories using essentials dynamic. The results indicate that changes in the structure of water by the effect of pressure and low temperatures destabilize the hydrophobic interaction modifying the solvation and the system volume leading to protein denaturation. Proteins 2016; 85:125-136. © 2016 Wiley Periodicals, Inc.
CEQUINOR (CONICET-UNLP), 120 e/61 y 62, Universidad Nacional de La Plata, La Plata, 1900, Argentina.
Yanis R
YR
Espinosa
CEQUINOR (CONICET-UNLP), 120 e/61 y 62, Universidad Nacional de La Plata, La Plata, 1900, Argentina.|Departmento de Biología, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, La Plata, 1900, Argentina.
J Raúl
JR
Grigera
Fundação Oswaldo Cruz., Rio de Janeiro, Programa de Computação Científica (PROCC), CEP, 21040-360, Rio de Janeiro, Brazil.
Ernesto R
ER
Caffarena
D003080:Cold Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D033862:Iron-Binding Proteins / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D011312:Pressure; D011489:Protein Denaturation; D000072417:Protein Domains; D017433:Protein Structure, Secondary; D058767:Protein Unfolding; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*; D000096923:Frataxin
D033862:Iron-Binding Proteins; D014867:Water; D000096923:Frataxin
cold denaturation; essential dynamics; hydrophobic interaction; molecular dynamics; water structure