Abstract

Many small biological objects, such as viruses, survive in a water environment and cannot remain active in dry air without condensation of water vapor. From a physical point of view, these objects belong to the mesoscale, where small thermal fluctuations with the characteristic kinetic energy of kBT (where kB is the Boltzmann’s constant and T is the absolute temperature) play a significant role. The self-assembly of viruses, including protein folding and the formation of a protein capsid and lipid bilayer membrane, is controlled by hydrophobic forces (i.e., the repulsing forces between hydrophobic particles and regions of molecules) in a water environment. Hydrophobic forces are entropic, and they are driven by a system’s tendency to attain the maximum disordered state. On the other hand, in information systems, entropic forces are responsible for erasing information, if the energy barrier between two states of a switch is on the order of kBT, which is referred to as Landauer’s principle. We treated hydrophobic interactions responsible for the self-assembly of viruses as an information-processing mechanism. We further showed a similarity of these submicron-scale processes with the self-assembly in colloidal crystals, droplet clusters, and liquid marbles.

Highlights

  • The recent COVID-19 pandemic has focused the attention of biophysicists and of the broad research community on viruses

  • From a physicist’s point of view, virus parFtrioclmesaarpehjyussitcnisatn’soppaorintitcloefs.vHieoww, evvireur,supnalirktiecles are ju engineered inorganic or organic nanopalritkiceleesn,gainweaetreerdeinnvoirrgoannmiceonrt iosrcgraunciicanl faonrovpiarrutsicelse.s, a wate Hydrophobic forces facilitated by waterrusaerse. rHesypdornopsihbolebifcofromrcoesstfasceillfi-taastseedmbbylyweaftfeercatsre respon throughout the life cycle of the virus

  • Since viruses do not maintain homeostasis, they re the thermal reservoir formed by an aquatic environment taing viruses is viewed as an important mechanism to lim destroyed due to protein denaturation

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Summary

Introduction

The recent COVID-19 pandemic has focused the attention of biophysicists and of the broad research community on viruses. Parts of viruses have common features with physico-chemical selfassembling supramolecular structures, such as micelles, liposomes, and vesicles This makes a thermodynamic analysis of the virus life cycle a significant objective for gaining general insights on self-assembly processes in physical chemistry. Earlier studies have suggested that viruses containing lipids are more viable in moist air than in dry air [4]. The latter seems clear because the viruses can serve as nuclei of condensation of water vapor. Entropy 2021, 23, 181 Entropy 2021, 23, 181 containing lipids are more viable in moist air than in dry air [4]

Protein Folding
Self-Assembly of Proteins and Lipids into Supramolecular Structures
Bio-Specific Interactions
The Information Life Cycle of a Virus
Conclusions
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