Abstract

Spatial models of the β - structures of protein molecules, forming layers of amino acids, in principle, of unlimited length for different conformations have been constructed. It is shown that the simplified flat Pauling models do not reflect the spatial structure of these layers. Using the recently developed theory of higher - dimensional polytopic prismahedrons, models of the volumetric filling of space with amino acid molecules are constructed. The constructed models for the first time mathematically describe the native structures of globular proteins. A model that simultaneously contains β - structures in parallel and anti - parallel positions and α - spirals. The turn of the polypeptide chain, which is often found in globular proteins, has been studied in higher dimensional space.

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