scholarly journals Structure for Energy Cycle: A unique status of Second Law of Thermodynamics for living systems

2018 ◽  
Author(s):  
Shu-Nong Bai ◽  
Hao Ge ◽  
Hong Qian

AbstractDistinguishing things from beings, or matters from lives, is a fundamental question. Extending E. Schrödinger’sneg-entropyand I. Prigogine’sdissipative structure, we propose a chemical kinetic view that the earliest “live” process is essentially a special interaction between a pair of specific components under a corresponding, particular environmental conditions. The interaction exists as an inter-molecular-force-bond complex (IMFBC) that couples two separate chemical processes: One is the spontaneous formation of an IMFBC driven by the decrease of Gibbs free energy as a dissipative process; while the other is the disassembly of the IMFBC driven thermodynamically by free energy input from the environment. The two processes that are coupled by the IMFBC were originated independently and considered non-living on Earth, but the IMFBC coupling of the two can be considered as the earliest form of metabolism: This forms the first landmark on the path from things to a being. The dynamic formation and dissemblance of the IMFBCs, as composite individuals, follows a principle designated as “… structure for energy for structure for energy…”, the cycle continues, shortly “structure for energy cycle”. With additional features derived from an IMFBC, such as multiple intermediates, autocatalytic ability of one individual upon the formation of another, aqueous medium, and mutual beneficial relationship between formation of polypeptides and nucleic acids, etc., the IMFBC-centered “live” process spontaneously evolved into more complex living organisms with the characteristics one currently knows.

Author(s):  
A. M. Savchenko ◽  
Yu. V. Konovalov ◽  
A. V. Laushkin

The relationship of the first and second laws of thermodynamics based on their energy nature is considered. It is noted that the processes described by the second law of thermodynamics often take place hidden within the system, which makes it difficult to detect them. Nevertheless, even with ideal mixing, an increase in the internal energy of the system occurs, numerically equal to an increase in free energy. The largest contribution to the change in the value of free energy is made by the entropy of mixing, which has energy significance. The entropy of mixing can do the job, which is confirmed in particular by osmotic processes.


Author(s):  
Claudio Giorgi ◽  
Angelo Morro

AbstractThe purpose of the paper is to establish vector-valued rate-type models for the hysteretic properties in deformable ferroelectrics within the framework of continuum thermodynamics. Unlike electroelasticity and piezoelectricity, in ferroelectricity both the polarization and the electric field are simultaneously independent variables so that the constitutive functions depend on both. This viewpoint is naturally related to the fact that an hysteresis loop is a closed curve in the polarization–electric field plane. For the sake of generality, the deformation of the material and the dependence on the temperature are allowed to occur. The constitutive functions are required to be consistent with the principle of objectivity and the second law of thermodynamics. Objectivity implies that the constitutive equations are form invariant within the set of Euclidean frames. Among other results, the second law requires a general property on the relation between the polarization and the electric field via a differential equation. This equation shows a dependence fully characterized by two quantities: the free energy and a function which is related to the dissipative character of the hysteresis. As a consequence, different hysteresis models may have the same free energy. Models compatible with thermodynamics are then determined by appropriate selections of the free energy and of the dissipative part. Correspondingly, major and minor hysteretic loops are plotted.


Entropy ◽  
2022 ◽  
Vol 24 (1) ◽  
pp. 94
Author(s):  
Mohammad Razavi ◽  
Seyed Majid Saberi Fathi ◽  
Jack Adam Tuszynski

The underlying mechanism determining the size of a particular cell is one of the fundamental unknowns in cell biology. Here, using a new approach that could be used for most of unicellular species, we show that the protein synthesis and cell size are interconnected biophysically and that protein synthesis may be the chief mechanism in establishing size limitations of unicellular organisms. This result is obtained based on the free energy balance equation of protein synthesis and the second law of thermodynamics. Our calculations show that protein synthesis involves a considerable amount of entropy reduction due to polymerization of amino acids depending on the cytoplasmic volume of the cell. The amount of entropy reduction will increase with cell growth and eventually makes the free energy variations of the protein synthesis positive (that is, forbidden thermodynamically). Within the limits of the second law of thermodynamics we propose a framework to estimate the optimal cell size at division.


2017 ◽  
Vol 19 (2) ◽  
pp. 1677-1685 ◽  
Author(s):  
Martin Brieg ◽  
Julia Setzler ◽  
Steffen Albert ◽  
Wolfgang Wenzel

Hydration free energy estimation of small molecules from all-atom simulations was widely investigated in recent years, as it provides an essential test of molecular force fields and our understanding of solvation effects.


Author(s):  
Rosa-Hilda Chavez ◽  
Jazmin Cortez-Gonzalez ◽  
Javier de J. Guadarrama ◽  
Abel Hernandez-Guerrero

The present paper describes the thermodynamic analysis of the carbon dioxide (CO2) gas removal process in two separated columns with absorption/stripping sections respectively. This process is characterized as mass transfer enhanced by chemical reaction, in which the presence of an alkanolamine enhances the solubility of an acid gas in the aqueous phase at a constant value of the equilibrium partial pressure. A very useful procedure for analyzing a process is by means of the Second Law of Thermodynamics. Thermodynamic analyses based on the concepts of irreversible entropy increase have frequently been suggested as pointers to sources of inefficiency in chemical processes. Furthermore, they point out where the irreversibilities of the process are located, and provide a generalized discussion from the successful application of the technique.


1968 ◽  
Vol 1 (2) ◽  
pp. 127-175 ◽  
Author(s):  
A. Katchalsky ◽  
R. Spangler

I. I. In his illuminating book onThe Nature of Thermodynamics, Bridgeman (1941) points out an intrinsic contradiction between the concepts of physical and biological evolution. In his words: ‘The view that the universe is running down into a condition where its entropy and the amount of disorder are as great as possible has had a profound effect on the views of many biologists on the nature of biological phenomena. It springs to the eye, however, that the tendency of living organisms is to organize their surroundings—that is to “produce” order where formerly there was disorder. Life then appears in some way to oppose the otherwise universal drive to disorder. Does it mean that living organisms do, or may violate the second law of thermodynamics?…’


2011 ◽  
Vol 366 (1580) ◽  
pp. 2949-2958 ◽  
Author(s):  
Robert Pascal ◽  
Laurent Boiteau

Thermodynamics provides an essential approach to understanding how living organisms survive in an organized state despite the second law. Exchanges with the environment constantly produce large amounts of entropy compensating for their own organized state. In addition to this constraint on self-organization, the free energy delivered to the system, in terms of potential, is essential to understand how a complex chemistry based on carbon has emerged. Accordingly, the amount of free energy brought about through discrete events must reach the strength needed to induce chemical changes in which covalent bonds are reorganized. The consequence of this constraint was scrutinized in relation to both the development of a carbon metabolism and that of translation. Amino acyl adenylates involved as aminoacylation intermediates of the latter process reach one of the higher free energy levels found in biochemistry, which may be informative on the range in which energy was exchanged in essential early biochemical processes. The consistency of this range with the amount of energy needed to weaken covalent bonds involving carbon may not be accidental but the consequence of the abovementioned thermodynamic constraints. This could be useful in building scenarios for the emergence and early development of translation.


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