By M. Volkenstein (Auth.)

ISBN-10: 0127230017

ISBN-13: 9780127230016

ISBN-10: 0127230025

ISBN-13: 9780127230023

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This is why it also repels negatively charged D N A and abandons it together with the positively charged histone. The free region of D N A capable of performing transcription in RNA remains [126]. The interaction of D N A and proteins in chromosomes results in the formation of a "superhelical" structure in which D N A molecules coagulate into chromatids with a considerable decrease of linear size. A number of models of the nucleohistone structure of chromatin have been suggested. Crick and Klug have put forth a model in which the coiling of DNA in chromatin is determined by a turn of the double helix approximately every twenty base pairs [130].

The key part played by proteases, according to Edelman, supports the explanation of facts discovered by Alexandrov. It should be emphasized that hypotheses to the effect that the specific interaction of similar supramolecular and cellular structures is determined by the specificity of micro- or macroscopic intermolecular forces, which have been widely discussed in the literature, cannot be regarded as convincing. These hypotheses were initially used to explain the synapsis of chromosomes; Jordan, one of the creators of quantum mechanics, held that quantum mechanical resonance forces operate between identical regions of two homologous chromosomes [74, 75].

In the proposed code, the six main amino acid residues (Ser, Tre, Asp, His, Gin, and Cis) and their sequence in the protein's stereospecific region determine the sequence of base pairs to which the given protein is mainly bound. The 40 1. M O L E C U L A R F O U N D A T I O N S O F BIOPHYSICS code, elaborated on the basis of stereochemistry, has been corroborated by the example of the interaction between Lac repressor and Lac operator (see p. 30 [134, 135], see also [136]. In this chapter we have dealt chiefly with the phenomena of molecular recognition, that is, specific interactions in biomolecular systems.

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General Biophysics by M. Volkenstein (Auth.)

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