Abstract

It is considered that the major process in an organism is the synthesis of the adenosine triphosphate (ATP) molecules (its resumption from the adenosine diphosphate (ADP) molecules). These molecules are the basic (if not unique) energy resource of an organism. For the completion of process of the ATP synthesis in mitochondria, it is necessary to transfer to it a pair of electrons from places where electrons rise up as a result of oxidizing processes. Research of mechanisms of such transfer is important therefore, in particular, from the point of regulative influence on them in medical aims.Various proteins, the primary structure of which can provide the transport of electrons between donors and acceptors, saturate a volume and membranes of cages. A question about a possibility to examine this primary structure of proteins as a nanowire of a semiconductor nature is analyzed. The possibility of active transport of electrons through its conductivity band is analyzed also.In this paper, it was shown that a heterogeneous protein system is possible to be considered as a semiconductor with an average-nitrogen nuclear subsystem and with an average-oxygen electronic subsystem. Also, it was shown that in the potential energy of interaction between the electron and the nuclear subsystem indeed exists non-compensated contributions. These contributions are related to the radicals and provide the active transport of electrons along the primary structure of protein molecules.It was demonstrated also that external fields can have local regulative influence on the transport of electron in proteins by compensating the remaining field or strengthening it.Fulfilled analysis gives a possibility in zero approximation of the application of representation of numbers of filling to the protein molecule, considering it as the nanowire.

Highlights

  • The detailed experimental and theoretical investigations showed that the energy structure of protein molecules in relation to the electronic states looks like enough typical for semiconductor crystals [1,2,3,4,5,6,7,8,9,10]

  • It is shown that even in the absence of the external field, the effective field is not equal to zero. It provides the active transport of electrons along the primary structure of the protein molecule

  • From all resulted approximations, presumably, most interesting is third. It is interesting because clearly demonstrate the presence of the spatially distributed residual electrostatic field conditioned by heterogeneity of amino acid composition of protein molecule

Read more

Summary

Background

The detailed experimental and theoretical investigations showed that the energy structure of protein molecules in relation to the electronic states looks like enough typical for semiconductor crystals [1,2,3,4,5,6,7,8,9,10]. All calculations listed above, as was mentioned in [9], were executed without taking into account of fact of amino acid heterogeneity of protein systems. The presence of unidentical radicals does not influence substantially on the electronic configuration of protein molecules, as radicals do not take part in the formation of the primary structure. As the calculations of the energy electronic structure of the real proteins are bulky enough, some farther analysis will be conducted in order to construct a model maximally close to the real protein molecule. It is shown that even in the absence of the external field, the effective field is not equal to zero It provides the active transport of electrons along the primary structure of the protein molecule. The external field creates a locally regulative influence on the electron transport

Methods
Results and discussion
V g0 m0 fg f 0 g0 nmn0
Conclusions

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.