Complementary hydropathy and the evolution of interacting polypeptides
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It has been shown that codons coding for strongly hydrophilic amino acids are complemented by codons that code for strongly hydrophobic ones, leading to a hypothesis stating that peptides thus encoded should interact. Though the principle has been validated in a number of experimental models, its general applicability has been questioned. I have discussed this principle, showing that the correlation between coding and noncoding strand amino acids was maintained, indeed slightly improved, when weighted averages based on codon usage tables were used to determine noncoding strand amino acid hydropathies. The coding capacity of the noncoding strand and its content of open reading frames were also discussed. Another point of contention that was afforded further clarification is the chemical plausibility of interactions between hydrophobic and hydrophilic amino acids implicit in this concept. The extension of complementary domains was also dealt with. Finally, I have discussed what I called the evolutionary drift of primary structure, and I showed as an example that though nucleotide sequences coding for the substance K receptor bear little resemblance to the inverse complement of that which codes for the SK peptide, a peptide spanning residues 130–139 is hydropathically very similar to that predicted from such an inverse complement.
Key wordsComplementary hydropathy Amino acid interactions Antisense coding capacity Coevolution of interacting proteins
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- Brentani RR, Pasqualini R (1990) Purification of the fibronectin receptor using the complementary hydropathy approach. In: Receptor purification. Humana Press (in press)Google Scholar
- Burley SK, Petsko GA (1988) Weakly polar interactions in proteins. In: Anfinsen CB, Edsall JT, Richards FM, Eisenberg DS (eds) Advances in protein chemistry, vol 39. pp 125–189Google Scholar
- Kunisawa T, Otsuka J (1987) A possible mode of protein evolution. The role of the anti-sense strand in the generation of new proteins. Protein Sequences & Data Anal 1:117–121Google Scholar
- Nemethy G, Scheraga HA (1967) The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins. J Am Chem Soc 66:1773–1789Google Scholar
- Ohno S (1981) Original domain for the serum albumin family arose from repeated sequences. Proc Natl Acad Sci USA 78:7657–7661Google Scholar
- Ohno S, Epplen JT (1983) The primitive code and repeats of base oligomers as the primordial protein-encoding sequence. Proc Natl Acad Sci USA 1983:3391–3395Google Scholar
- Poland D, Scheraga HA (1967) In: Fasman G (ed) Poly-α-aminoacids. Marcel Dekker, New York, pp 481–483Google Scholar