2019
DOI: 10.1038/s41598-019-50443-2
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Saving Old Bones: a non-destructive method for bone collagen prescreening

Abstract: Bone collagen is an important material for radiocarbon, paleodietary, and paleoproteomic analyses, but it degrades over time, making such analyses more difficult with older material. Collagen preservation between and within archaeological sites is also variable, so that much time, effort, and money can go into the preparation and initial analysis of samples that will not yield meaningful results. To avoid this, various methods are employed to prescreen bone for collagen preservation (e.g., %N, microporosity, a… Show more

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Cited by 45 publications
(26 citation statements)
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“…However, even if DNA decay accelerates with increasing collagen hydrolysis, screening archaeological bone using collagen analysis is typically a destructive method, (but see the recent report of the successful use of near-infrared [72]) is also relatively time-consuming and labour-intensive, while the widespread use of an additional ultrafiltration step can have a strong influence on the collagen yields [73][74][75]. Therefore, while collagen yield seems to be an effective method to predict endogenous DNA content, it is most useful as an additional…”
Section: Plos Onementioning
confidence: 99%
“…However, even if DNA decay accelerates with increasing collagen hydrolysis, screening archaeological bone using collagen analysis is typically a destructive method, (but see the recent report of the successful use of near-infrared [72]) is also relatively time-consuming and labour-intensive, while the widespread use of an additional ultrafiltration step can have a strong influence on the collagen yields [73][74][75]. Therefore, while collagen yield seems to be an effective method to predict endogenous DNA content, it is most useful as an additional…”
Section: Plos Onementioning
confidence: 99%
“…Despite its potential, few studies have used spectroscopic techniques to determine collagen preservation in archaeological bone [21][22][23][24][25] . Fourier Transform Infrared (FTIR) spectroscopy has been regarded as a suitable method to explore the structure of collagen [26][27][28][29][30][31][32] , by relating FTIR absorption bands (of the amide I, II and III) to specific chemical bonds and secondary structural features (α-helix, β-sheets, β-turns and random coils), even in the most recent investigations 32 .…”
mentioning
confidence: 99%
“…It is always good practice to (pre)screen samples for collagen preservation [ 107 ]. Methods and metrics include percentage yield of collagen after each pretreatment step, atomic C : N (carbon : nitrogen) ratios, stable C and N isotope values [ 29 ], whole-bone %N [ 108 ] and, less frequently, relatively expensive but extremely quantitative HPLC [ 47 , 48 , 109 ] and near-infrared spectroscopic methods [ 110 ]. Several respondents (#11, 16, 50, 67, 121 and 127: electronic supplementary material, appendix SC, table S2) remarked the importance of those quality indicators in routine research work using 14 C data.…”
Section: Discussionmentioning
confidence: 99%