Published October 30, 2019
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Figure 3 in Mechanisms of soft tissue and protein preservation in Tyrannosaurus rex
Creators
- 1. Department of Engineering, Wake Forest University, Winston Salem, NC, 27101, USA
- 2. Museum of Paleontology, University of California, Berkeley, CA, 94720, USA
- 3. Advanced Light Source, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA
- 4. Department of Biological Sciences, North Carolina State University, Raleigh, NC, 27695, USA
- 5. Department of Materials Science and Engineering, University of California, Berkeley, CA, 94720, USA
- 6. Department of Biological Sciences, North Carolina State University, Raleigh, NC, 27695, USA. Department of Geology, Lund University, Lund, Sweden. North Carolina Museum of Natural Sciences, Raleigh, NC, 27601, USA. Museum of the Rockies, Montana State University, Bozeman, MT, 59715, USA
Description
Figure 3. SR-FTIR full spectra of isolated T. rex vascular tissue and chicken type I collagen (no treatment). All key bands for the identification of protein (Amide I, Amide II, Amide III) are present in the dinosaur tissue spectrum. The T. rex spectrum also presents a strong non-peptide carbonyl (C=O) band at 1739 cm−1 and a carbohydrate band at ~1010 cm−1.
Notes
Published as part of Elizabeth M. Boatman, Mark B. Goodwin, Hoi-Ying N. Holman, Sirine F akra, Wenxia Zheng, Ronald Gronsky & Mary H. Schweitzer, 2019, Mechanisms of soft tissue and protein preservation in Tyrannosaurus rex, pp. 1-12 in Scientific Reports (15678) 9 on page 5, DOI: 10.1038/s41598-019-51680-1, http://zenodo.org/record/3748973
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