Abstract

Key features of the structures of globular proteins are considered to show to what extent they demand the specific amino acid sequences strategically selected during biological evolution. It is shown that: (a) the length distributions of α- and β-regions in water-soluble globular proteins are similar to what can be expected for a random copolymer of polar and nonpolar residues; (b) the alteration of α- and β-regions in globular proteins is similar to that of the random one; (c) typical folding patterns (i.e., crude three-dimensional structures) of globular proteins coincide with the thermodynamically most stable folding patterns of random sequences (and even of chemically homogeneous polypeptides with unpolar side groups). The possibility cannot be excluded that even the tight packing inside protein molecules (making the protein molecule stable relative to thermal fluctuations) does not demand a very strict selection of amino acid sequences. The conclusion is drawn that primary structures of proteins are basically just the examples of random amino acid sequences which have only been “edited” during biological evolution in order to impart to them the additional (functional) meaning and the additional stability.

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