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Protein sequences bound to mineral surfaces persist into deep time

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  • Shaun Hall
  • Teresa Roncal-Herrero
  • Colin Freeman
  • Jos Woolley
  • Molly Katherine Crisp
  • Anna Fotakis
  • Roman Fischer
  • Benedikt Kessler
  • Rosa Rakownikow Jersie-Christensen
  • Jesper Olsen
  • James Haile
  • Jessica Thomas
  • Curtis Marean
  • John Parkington
  • Samantha Louise Presslee
  • Julia Lee-Thorp
  • Peter Ditchfield
  • Terry Harrison
  • Manuel Dominguez-Rodrigo
  • Ross MacPhee
  • Amandus Kwekason
  • Michaela Ecker
  • Liora Kolska Horwitz
  • Michael Chazan
  • John Harding
  • Enrico Cappellini


Publication details

DateAccepted/In press - 17 Aug 2016
DatePublished (current) - 27 Sep 2016
Issue numberSeptember
Number of pages50
Pages (from-to)1-50
Original languageEnglish


Proteins persist longer in the fossil record than DNA, but the longevity, survival mechanisms and substrates remain contested. Here, we demonstrate the role of mineral binding in preserving the protein sequence in ostrich (Struthionidae) eggshell, including from the palaeontological sites of Laetoli (3.8 Ma) and Olduvai Gorge (1.3 Ma) in Tanzania. By tracking protein diagenesis back in time we find consistent patterns of preservation, demonstrating authenticity of the surviving sequences. Molecular dynamics simulations of struthiocalcin-1 and -2, the dominant proteins within the eggshell, reveal that distinct domains bind to the mineral surface. It is the domain with the strongest calculated binding energy to the calcite surface that is selectively preserved. Thermal age calculations demonstrate that the Laetoli and Olduvai peptides are 50 times older than any previously authenticated sequence (equivalent to ~16 Ma at a constant 10 ̊C).


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