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Science 9 March 1979:
Vol. 203. no. 4384, pp. 1012 - 1014
DOI: 10.1126/science.106468
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Articles

Science, Vol 203, Issue 4384, 1012-1014
Copyright © 1979 by American Association for the Advancement of Science

articles

beta-Galactosidase and selective neutrality

R Holmquist

Three hypotheses to explain the amino acid composition of proteins are inconsistent (P congruent to 10(-9) with the experimental data for beta-galactosidase from Escherichia coli. The exceptional length of this protein, 1021 residues, permits rigorous tests of these hypotheses without complication from statistical artifacts. Either this protein is not at compositional equilibrium, which is unlikely from knowledge about other proteins, or the evolution of this protein and its coding gene have not been selectively neutral. However, the composition of approximately 60 percent of the molecule is consistent with either a selectively neutral or nonneutral evolutionary process.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Beta-galactosidase and selective neutrality.
R Holmquist and T Conroy (1979)
Science 206, 235
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