Statistical distribution of hydrophobic residues along the length of protein chains. Implications for protein folding and evolution.
We consider in this paper the statistical distribution of hydrophobic residues along the length of protein chains. For this purpose we used a binary hydrophobicity scale which assigns hydrophobic residues a value of one and non-hydrophobes a value of zero. The resulting binary sequences are tested for randomness using the standard run test. For the majority of the 5,247 proteins examined, the distribution of hydrophobic residues along a sequence cannot be distinguished from that expected for a random distribution. This suggests that (a) functional proteins may have originated from random sequences, (b) the folding of proteins into compact structures may be much more permissive with less sequence specificity than previously thought, and (c) the clusters of hydrophobic residues along chains which are revealed by hydrophobicity plots are a natural consequence of a random distribution and can be conveniently described by binomial statistics.
Department of Physiology and Biophysics, University of California, Irvine 92717.
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White
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Jacobs
D000596:Amino Acids; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D005075:Biological Evolution; D006217:Halobacterium / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007256:Information Systems; D046911:Macromolecular Substances; D045322:Photosynthetic Reaction Center Complex Proteins; D011487:Protein Conformation; D011506:Proteins / Q000235:genetics / Q000378:metabolism; D011897:Random Allocation; D012242:Rhodobacter sphaeroides / Q000235:genetics / Q000378:metabolism; D012241:Rhodopseudomonas / Q000235:genetics / Q000378:metabolism
D000596:Amino Acids; D001426:Bacterial Proteins; D046911:Macromolecular Substances; D045322:Photosynthetic Reaction Center Complex Proteins; D011506:Proteins