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description Publicationkeyboard_double_arrow_right Article , Other literature type 2016 Italy, United Kingdom, United Kingdom, Denmark, FranceeLife Sciences Publications, Ltd UKRI | E-Infrastructure Intercon..., SSHRC, NSF | Paleonanthropological Res... +7 projectsUKRI| E-Infrastructure Interconnectivity EPSRC - Chris Taylor ,SSHRC ,NSF| Paleonanthropological Research in the Laetoli Area, Tanzania ,UKRI| Building a Better Egg Timer? ,EC| MAARITIME ,NSF| Doctoral Dissertation Improvement-Paleoecology of the Upper Laetolil Beds, Laetoli, Tanzania: Its Implications for Hominid Evolution ,NSF| Continued Paleoanthropological Research in the Laetoli area, Tanzania ,EC| SMILEY ,NSF| IPG - Developing and Testing an Integrated Paleoscape Model for the early Middle and Late Pleistocene of the South Coast of South Africa ,UKRI| Hard-soft matter interfaces: from understanding to engineeringBeatrice Demarchi; Shaun Hall; Teresa Roncal-Herrero; Colin L. Freeman; Jos Woolley; Molly Crisp; Julie Wilson; Anna K. Fotakis; Roman Fischer; Benedikt M. Kessler; Rosa Rakownikow Jersie-Christensen; Jesper V. Olsen; James Haile; Jessica E. Thomas; Curtis W. Marean; John Parkington; Samantha Presslee; Julia A. Lee-Thorp; Peter Ditchfield; Jacqueline F. Hamilton; Martyn W. Ward; Chunting Michelle Wang; Marvin D. Shaw; Terry Harrison; Manuel Domínguez-Rodrigo; Ross D. E. MacPhee; Amandus Kwekason; Michaela Ecker; Liora Kolska Horwitz; Michael Chazan; Roland Kröger; Jane Thomas-Oates; John H. Harding; Enrico Cappellini; Kirsty Penkman; Matthew J. Collins;eLife digest The pattern of chemical reactions that break down the molecules that make our bodies is still fairly mysterious. Archaeologists and geologists hope that dead organisms (or artefacts made from them) might not decay entirely, leaving behind clues to their lives. We know that some molecules are more resistant than others; for example, fats are tough and survive for a long time while DNA is degraded very rapidly. Proteins, which are made of chains of smaller molecules called amino acids, are usually sturdier than DNA. Since the amino acid sequence of a protein reflects the DNA sequence that encodes it, proteins in fossils can help researchers to reconstruct how extinct organisms are related in cases where DNA cannot be retrieved. Time, temperature, burial environment and the chemistry of the fossil all influence how quickly a protein decays. However, it is not clear what mechanisms slow down decay so that full protein sequences can be preserved and identified after millions of years. As a result, it is difficult to know where to look for these ancient sequences. In the womb of ostriches, several proteins are responsible for assembling the minerals that make up the ostrich eggshell. These proteins become trapped tightly within the mineral crystals themselves. In this situation, proteins can potentially be preserved over geological time. Demarchi et al. have now studied 3.8 million-year-old eggshells found close to the equator and, despite the extent to which the samples have degraded, discovered fully preserved protein sequences. Using a computer simulation method called molecular dynamics, Demarchi et al. calculated that the protein sequences that are able to survive the longest are stabilized by strong binding to the surface of the mineral crystals. The authenticity of these sequences was tested thoroughly using a combination of several approaches that Demarchi et al. recommend using as a standard for ancient protein studies. Overall, it appears that biominerals are an excellent source of ancient protein sequences because mineral binding ensures survival. A systematic survey of fossil biominerals from different environments is now needed to assess whether these biomolecules have the potential to act as barcodes for interpreting the evolution of organisms. DOI: http://dx.doi.org/10.7554/eLife.17092.002 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). DOI: http://dx.doi.org/10.7554/eLife.17092.001
Archivio Istituziona... arrow_drop_down Oxford University Research ArchiveOther literature type . 2016License: CC BYData sources: Oxford University Research ArchiveArchiMer - Institutional Archive of IfremerOther literature type . 2016Data sources: ArchiMer - Institutional Archive of IfremerCopenhagen University Research Information SystemArticle . 2016Data sources: Copenhagen University Research Information Systemadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.7554/elife.17092&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu169 citations 169 popularity Top 1% influence Top 10% impulse Top 1% Powered by BIP!visibility 29visibility views 29 download downloads 178 Powered bymore_vert Archivio Istituziona... arrow_drop_down Oxford University Research ArchiveOther literature type . 2016License: CC BYData sources: Oxford University Research ArchiveArchiMer - Institutional Archive of IfremerOther literature type . 2016Data sources: ArchiMer - Institutional Archive of IfremerCopenhagen University Research Information SystemArticle . 2016Data sources: Copenhagen University Research Information Systemadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.7554/elife.17092&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euResearch data keyboard_double_arrow_right Dataset 2017 United KingdomThe University of Sheffield NSF | Paleonanthropological Res..., SSHRC, NSF | Doctoral Dissertation Imp... +7 projectsNSF| Paleonanthropological Research in the Laetoli Area, Tanzania ,SSHRC ,NSF| Doctoral Dissertation Improvement-Paleoecology of the Upper Laetolil Beds, Laetoli, Tanzania: Its Implications for Hominid Evolution ,NSF| IPG - Developing and Testing an Integrated Paleoscape Model for the early Middle and Late Pleistocene of the South Coast of South Africa ,EC| SMILEY ,EC| MAARITIME ,UKRI| Hard-soft matter interfaces: from understanding to engineering ,UKRI| E-Infrastructure Interconnectivity EPSRC - Chris Taylor ,UKRI| Building a Better Egg Timer? ,NSF| Continued Paleoanthropological Research in the Laetoli area, TanzaniaAuthors: Harding, John; Hall, Shaun; Freeman, Colin;Harding, John; Hall, Shaun; Freeman, Colin;Sample input files of molecular dynamics calculations and pdb files of proteins and peptides, associated with paper: Demarchi et al. (2016) Protein sequences bound to mineral surfaces persist into deep time. eLife 2016;5:e17092. DOI: 10.7554/eLife.17092Proteins 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).
ORDA - The Universit... arrow_drop_down ORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: DataciteORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: Dataciteadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.15131/shef.data.3491387.v1&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu0 citations 0 popularity Average influence Average impulse Average Powered by BIP!more_vert ORDA - The Universit... arrow_drop_down ORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: DataciteORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: Dataciteadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.15131/shef.data.3491387.v1&type=result"></script>'); --> </script>
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description Publicationkeyboard_double_arrow_right Article , Other literature type 2016 Italy, United Kingdom, United Kingdom, Denmark, FranceeLife Sciences Publications, Ltd UKRI | E-Infrastructure Intercon..., SSHRC, NSF | Paleonanthropological Res... +7 projectsUKRI| E-Infrastructure Interconnectivity EPSRC - Chris Taylor ,SSHRC ,NSF| Paleonanthropological Research in the Laetoli Area, Tanzania ,UKRI| Building a Better Egg Timer? ,EC| MAARITIME ,NSF| Doctoral Dissertation Improvement-Paleoecology of the Upper Laetolil Beds, Laetoli, Tanzania: Its Implications for Hominid Evolution ,NSF| Continued Paleoanthropological Research in the Laetoli area, Tanzania ,EC| SMILEY ,NSF| IPG - Developing and Testing an Integrated Paleoscape Model for the early Middle and Late Pleistocene of the South Coast of South Africa ,UKRI| Hard-soft matter interfaces: from understanding to engineeringBeatrice Demarchi; Shaun Hall; Teresa Roncal-Herrero; Colin L. Freeman; Jos Woolley; Molly Crisp; Julie Wilson; Anna K. Fotakis; Roman Fischer; Benedikt M. Kessler; Rosa Rakownikow Jersie-Christensen; Jesper V. Olsen; James Haile; Jessica E. Thomas; Curtis W. Marean; John Parkington; Samantha Presslee; Julia A. Lee-Thorp; Peter Ditchfield; Jacqueline F. Hamilton; Martyn W. Ward; Chunting Michelle Wang; Marvin D. Shaw; Terry Harrison; Manuel Domínguez-Rodrigo; Ross D. E. MacPhee; Amandus Kwekason; Michaela Ecker; Liora Kolska Horwitz; Michael Chazan; Roland Kröger; Jane Thomas-Oates; John H. Harding; Enrico Cappellini; Kirsty Penkman; Matthew J. Collins;eLife digest The pattern of chemical reactions that break down the molecules that make our bodies is still fairly mysterious. Archaeologists and geologists hope that dead organisms (or artefacts made from them) might not decay entirely, leaving behind clues to their lives. We know that some molecules are more resistant than others; for example, fats are tough and survive for a long time while DNA is degraded very rapidly. Proteins, which are made of chains of smaller molecules called amino acids, are usually sturdier than DNA. Since the amino acid sequence of a protein reflects the DNA sequence that encodes it, proteins in fossils can help researchers to reconstruct how extinct organisms are related in cases where DNA cannot be retrieved. Time, temperature, burial environment and the chemistry of the fossil all influence how quickly a protein decays. However, it is not clear what mechanisms slow down decay so that full protein sequences can be preserved and identified after millions of years. As a result, it is difficult to know where to look for these ancient sequences. In the womb of ostriches, several proteins are responsible for assembling the minerals that make up the ostrich eggshell. These proteins become trapped tightly within the mineral crystals themselves. In this situation, proteins can potentially be preserved over geological time. Demarchi et al. have now studied 3.8 million-year-old eggshells found close to the equator and, despite the extent to which the samples have degraded, discovered fully preserved protein sequences. Using a computer simulation method called molecular dynamics, Demarchi et al. calculated that the protein sequences that are able to survive the longest are stabilized by strong binding to the surface of the mineral crystals. The authenticity of these sequences was tested thoroughly using a combination of several approaches that Demarchi et al. recommend using as a standard for ancient protein studies. Overall, it appears that biominerals are an excellent source of ancient protein sequences because mineral binding ensures survival. A systematic survey of fossil biominerals from different environments is now needed to assess whether these biomolecules have the potential to act as barcodes for interpreting the evolution of organisms. DOI: http://dx.doi.org/10.7554/eLife.17092.002 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). DOI: http://dx.doi.org/10.7554/eLife.17092.001
Archivio Istituziona... arrow_drop_down Oxford University Research ArchiveOther literature type . 2016License: CC BYData sources: Oxford University Research ArchiveArchiMer - Institutional Archive of IfremerOther literature type . 2016Data sources: ArchiMer - Institutional Archive of IfremerCopenhagen University Research Information SystemArticle . 2016Data sources: Copenhagen University Research Information Systemadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.7554/elife.17092&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu169 citations 169 popularity Top 1% influence Top 10% impulse Top 1% Powered by BIP!visibility 29visibility views 29 download downloads 178 Powered bymore_vert Archivio Istituziona... arrow_drop_down Oxford University Research ArchiveOther literature type . 2016License: CC BYData sources: Oxford University Research ArchiveArchiMer - Institutional Archive of IfremerOther literature type . 2016Data sources: ArchiMer - Institutional Archive of IfremerCopenhagen University Research Information SystemArticle . 2016Data sources: Copenhagen University Research Information Systemadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.7554/elife.17092&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.euResearch data keyboard_double_arrow_right Dataset 2017 United KingdomThe University of Sheffield NSF | Paleonanthropological Res..., SSHRC, NSF | Doctoral Dissertation Imp... +7 projectsNSF| Paleonanthropological Research in the Laetoli Area, Tanzania ,SSHRC ,NSF| Doctoral Dissertation Improvement-Paleoecology of the Upper Laetolil Beds, Laetoli, Tanzania: Its Implications for Hominid Evolution ,NSF| IPG - Developing and Testing an Integrated Paleoscape Model for the early Middle and Late Pleistocene of the South Coast of South Africa ,EC| SMILEY ,EC| MAARITIME ,UKRI| Hard-soft matter interfaces: from understanding to engineering ,UKRI| E-Infrastructure Interconnectivity EPSRC - Chris Taylor ,UKRI| Building a Better Egg Timer? ,NSF| Continued Paleoanthropological Research in the Laetoli area, TanzaniaAuthors: Harding, John; Hall, Shaun; Freeman, Colin;Harding, John; Hall, Shaun; Freeman, Colin;Sample input files of molecular dynamics calculations and pdb files of proteins and peptides, associated with paper: Demarchi et al. (2016) Protein sequences bound to mineral surfaces persist into deep time. eLife 2016;5:e17092. DOI: 10.7554/eLife.17092Proteins 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).
ORDA - The Universit... arrow_drop_down ORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: DataciteORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: Dataciteadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.15131/shef.data.3491387.v1&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu0 citations 0 popularity Average influence Average impulse Average Powered by BIP!more_vert ORDA - The Universit... arrow_drop_down ORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: DataciteORDA - The University of Sheffield Research Data Catalogue and RepositoryDataset . 2017License: CC BYData sources: Dataciteadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.15131/shef.data.3491387.v1&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eu