Abstract
The distribution of point mutations accepted by natural selection in the amino acid sequences of 16 cytochrome-C, 7 lysozyme, 15 myoglobin, 10 ribonuclease, 12 short neurotoxin, 16 plant ferredoxin and 6 bacterial ferredoxin molecules have been investigated. The number of point mutations shows an increasing tendency from the NH 2-terminus towards the COON-terminus of these proteins or at least within their structural domains. Our results suggest that the continuous folding of polypeptide chain during biosynthesis may play an important role in the formation of globular protein structure.
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