The Study Of The Kinetics And Thermodynamics Of The Flexible Proteins Folding And Binding

Since Anfinsen and his co-workers brought forward the plus of the stability of thermodynamics is the right folding drive in the protein folding process basis on the study of the reversible ribotide-enzyme stretch and refold in 1960s, the investigation on the study of kinetics and thermodynamics of protein folding and binding have been greatly promoted. Especially the theory of the energy landscapes that were established by P. G Wolynes offered a powerful theory model for protein folding and binding in biophysics. People have made great progress on kinetics and thermodynamics of protein folding and binding since 1990s, and have given new physics understanding and theoretical results^[1-5].In this paper, we study the influence on the rate of protein folding and binding both in two dimension and three dimension. We study the rate of protein folding and binding at different temperature, different folding energy and different length of protein. Then we find the rule of kinetics and thermodynamics of protein folding and binding. What's more, we formulate the expression of the free energy of three dimension.Through studying the evolution of protein folding and binding probability with time, we find that there is an optimal temperature. At this temperature, the rate of protein folding and binding is the fastest of all, and the time of the system reaching its native state is the shortest. As the temperature increases, the proteins become less and less stable, and the non-native unfolding and binding states are more and more preferred. Therefore the time it takes to reach the native state is longer. On the other hand, as the temperature decreases, the time it takes to reach the native folding-binding state is also longer. This is because it is more and more likely that the protein will be trapped into some low-lying energy states. This phenomenon was observed in many experiments. It was proved that the energy landscape is very useful in rationalizing many details of the folding phenomenon again. It will help design experiments too. This is just about the meaning of the paper.