Conformational temperature characterizing the folding of a protein.
The time sequences of the molecular dynamics simulation for the folding process of a protein is analyzed with the inherent structure landscape which focuses on the configurational dynamics of the system. Time-dependent energy and entropy for inherent structures are introduced, and from these quantities a conformational temperature is defined. The conformational temperature follows the time evolution of a slow relaxation process and reaches the bath temperature when the system is equilibrated. We show that the nonequilibrium system is described by two temperatures, one for fast vibration and the other for slow configurational relaxation, while the equilibrium system is described by one temperature. The proposed formalism is applicable widely for systems with many metastable states.
Nakagawa
Naoko
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College of Science, Ibaraki University, Mito, Ibaraki 310-8512, Japan.
D000465:Algorithms; D019277:Entropy; D015233:Models, Statistical; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature