Quantitative Criteria of Chirality in Hierarchical Protein Structures

Biophysics - Based on the theory of the formation of sign-alternating hierarchical structures in macromolecular systems, a quantitative approach was developed to assess the chirality sign of...     

The Relationship between Hierarchical Chiral Structures of Proteins and their Functions

Biophysics - The specific characteristics of the distribution of secondary structures and coiled-coil superhelix structures were investigated for the first time, while taking the sign of chirality...     

Stimulation of the Growth of Juvenile North African Catfish Clarias gariepinus by Modification of the Water Oxidation–Reduction Potential

Biology Bulletin - The effect of water with a high negative oxidation–reduction potential (ORP) on the physiological parameters of juvenile North African catfish (Clarias gariepinus) has been...     

Methods to Determine the Chirality Sign for Helical and Superhelical Protein Structures

Biophysics - A method was designed to describe the helical structures of various levels of organization in proteins. The method makes it possible to characterize the sign of chirality/helicity and...     

The Influence of a Deuterium Depleted Drinking Diet on the Functional State of the Central Nervous System of Animals in Hypoxia

Biophysics - The effects of prolonged (42 day) consumption of deuterium-depleted water by rats on the functional state of their central nervous system under normal conditions and under conditions...     

The Mechanisms of the Interaction of Stable Isotopes with Biological Objects in the Presence of an Uncompensated Neutron in Chemical Bonds

The physical regularities that lead to isotope fractionation and to the accumulation of certain isotope forms in the intercellular and intracellular space at various levels of biological objects were studied. A new hypothesis of fractionation of stable isotopes in biological objects through the neutron effect was discussed. The following feature is noted: it is very likely that the development of isotope shock in living beings is observed mainly in the presence of covalent bonds between atoms with an uncompensated neutron. One possible explanation for this phenomenon can be associated with a change in the physical parameters of the following events: the interactions of the magnetic moments of valence electrons with the magnetic moments of atomic nuclei and the interactions of magnetic moments of atomic nuclei, which result in a change in the distance between atomic nuclei.

     

A periodic system of chiral structures in molecular biology

A systemic regularity of molecular biology is considered: the tendency towards alternating of the sense of chirality of intramolecular structural levels of DNA and proteins, namely, D–L–D–L for DNA and L–D–L–D for proteins, is observable starting from the level of asymmetric carbon in deoxyribose and amino acids. Helicity is a special case of chirality. In intermolecular interactions, the sense of chirality of the highest intramolecular structural level directly involved in the interaction prevails in each of the participants. The interaction of molecules of the same nature (protein–protein, DNA–RNA, tRNA–mRNA, and ribozymes) mainly occurs in the case of the same sense of chirality, either L–L or D–D, and for molecules of different types (DNA–protein, tRNA–amino acids, and enzyme–substrate), in the case of different senses of chirality, either D–L or L–D. An alternating sense of the chiral hierarchy of conjugated levels of macromolecular structures in proteins and nucleic acids is of general biological importance: it determines the discreteness of levels, serves as a tool of folding, and provides a structural basis for “preferred collective” (or “macroscopic mechanical”) degrees of freedom in the design of macromolecular machines, as well as being one of the mechanisms of blockwise/saltatory development of the evolutionary process. A new fundamental concept is proposed: the homochirality of primary structures of DNA and proteins determines the amount of the entropic component of the free energy, which is used in the processes of folding and molecular rearrangements.