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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jcsc/111/01/0081-0086

    • Keywords

       

      Triple helix; stabilization; evolution

    • Abstract

       

      Sequences with glycine in every third position have been detected in DNA derived sequences of proteins in phages and bacteria and it was suggested that these regions trimerise to collagenous structures. Related sequences are found in proteins of mollusks and slime mold. The sequences contain a much lower fraction of proline than mammalian collagens and it is unknown how many of the prolines, if any, are converted to hydroxyproline. Therefore, for triple helix formation other stabilizing interactions than those known for mammalian collagens are required. Strikingly, aspartate and asparagine are abundant in collagen-like sequences of phage tail fibre proteins and of related sequences in nacrein of oyster pearls suggesting a possible stabilization by calcium binding.

    • Author Affiliations

       

      Juergen Engel1 Hans Peter Bächinger2

      1. Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstr. 70, Basel - CH-4056, Switzerland
      2. Research Unit, Shriners Hospital for Children and the Department of Biochemistry and Molecular Biology, Oregon Health Science University, Portland, Oregon - 97201, USA

    • Dates

       
      Published
      February 1999

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