Journal of Thermodynamics & Catalysis
Open Access

Mechanism of Thermodynamics in Bimolecular System

Huaying Zhao^{* *}Correspondence: Huaying Zhao, Department of Chemical Engineering and Macromolecular Biophysics, Millersville University, Dilworth Rd, Millersville, USA, Email:

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Description

Thermodynamics is a branch of science that deals with the study of energy and its transformations in various physical and chemical systems. It is an essential tool for understanding the behavior of bio molecular systems, including the biochemical reactions that take place in living organisms. This article highlights about the principles of thermodynamics and how they apply to bio molecular systems. The first law of thermodynamics states that energy cannot be created or destroyed only transformed from one form to another. In biomolecular systems, this means that the energy required for biochemical reactions comes from the environment, such as the food that is eaten.

The energy is then transformed into chemical energy in the form of Adenosine Triphosphate (ATP), which is used to power various cellular processes. The second law of thermodynamics states that in any energy transformation, there will always be some loss of energy in the form of heat. In biomolecular systems, this means that not all of the energy released in a reaction can be used for work. Some of the energy is always lost as heat, which is why biochemical reactions are not 100% efficient. In addition to these fundamental laws, there are also several thermodynamic parameters that are used to describe the behavior of biomolecular systems. These parameters include enthalpy, entropy, and free energy. Enthalpy is a measure of the heat content of a system.

It is the sum of the internal energy of the system and the product of the pressure and volume. In biomolecular systems, enthalpy is important for understanding the energy changes that occur during biochemical reactions. For example, an exothermic reaction releases heat, resulting in a negative change in enthalpy. Entropy is a measure of the disorder or randomness of a system. In biomolecular systems, entropy is important for understanding the degree of organization within a cell. For example, a highly organized protein structure will have low entropy, while a disordered protein structure will have high entropy.

Free energy is a measure of the energy available to do work in a system. It is calculated as the difference between the enthalpy and entropy of a system. In biomolecular systems, free energy is important for understanding the direction and spontaneity of biochemical reactions. A negative change in free energy indicates that a reaction is spontaneous and releases energy, while a positive change in free energy indicates that a reaction is nonspontaneous and requires energy input.

One of the key applications of thermodynamics in biomolecular systems is the study of enzyme-catalyzed reactions. Enzymes are biological catalysts that accelerate the rate of biochemical reactions by lowering the activation energy required for the reaction to occur. The rate of an enzyme-catalyzed reaction can be described using the Michaelis-Menten equation, which relates the rate of the reaction to the concentration of the substrate.

Conclusion

The Michaelis-Menten equation is based on the principles of thermodynamics. The rate of the reaction is dependent on the free energy change of the reaction, which in turn is determined by the concentrations of the reactants and products. The enzyme acts to lower the activation energy of the reaction, which increases the rate of the reaction by increasing the number of molecules that have sufficient energy to react. Another important application of thermodynamics in biomolecular systems is the study of protein folding. Proteins are large, complex molecules that are responsible for carrying out many of the functions within a cell. The structure of a protein is critical for its function, and improper folding can lead to disease. Protein folding is a complex process that is determined by a number of thermodynamic factors. The stability of a protein is determined by the balance between the enthalpy and entropy of the system. The enthalpy of a protein is determined by the strength of the chemical bonds that hold the protein together.