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β-Galactosidase from Osmotic Remedial Lactose Utilization Mutants of E. Coli

  • R. T. Vinopal
  • S. A. Wartell
  • K. S. Kolowsky
Part of the Basic Life Sciences book series (BLSC, volume 14)

Abstract

Retrieval of genetic information for synthesis of an enzyme is usually thought of in terms of transfer of sequence information — transcription of the base sequence of the gene into mRNA and translation of mRNA into the amino acid sequence of the polypeptide chain. The final expression of the gene, folding of the polypeptide to form the biologically active globular protein, is considered to result automatically from the sequence of amino acids. An information specialist will point out that the amino acid sequence does not possess enough information to specify the precisely folded shape of the active enzyme. The additional information comes from the specification of the environment in which the polypeptide folds. Anfinsen (1973) describes the thermodymanic hypothesis for protein folding in this way: “This hypothesis states that the three-dimensional structure of a native protein in its normal physiological milieu (solvent, pH, ionic strength, presence of other components such as metal ions or prosthetic groups, temperature, and other) is the one in which the Gibbs free energy of the whole system is the lowest; that is, that the native conformation is determined by the totality of interatomic interactions and hence by the amino acid sequence in a given environment. In terms of natural selection through the ‘design’ of macromolecule during evolution, this idea emphasizes the fact that a protein molecule only makes stable structural sense when it exist under conditions similar to those for which it was selected — the so-called physiological state.”

Keywords

Compatible Solute Monovalent Cation Neurospora Crassa Osmotic Concentration Lactose Utilization 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • R. T. Vinopal
    • 1
  • S. A. Wartell
    • 1
  • K. S. Kolowsky
    • 1
  1. 1.Microbiology Section, U-44 Biological Sciences GroupUniversity of ConnecticutStorrsUSA

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