scholarly journals Proteomic profile of bone “collagen” extracted for stable isotopes: implications for bulk and single amino acid analyses

Author(s):  
Timothy P. Cleland ◽  
Julianne J. Sarancha ◽  
Christine A.M. France
2002 ◽  
Vol 24 (3) ◽  
pp. 12-14 ◽  
Author(s):  
Christina Nielsen-Marsh

Svante Pääbo, a leading pioneer in the study of ancient DNA, eloquently described the recovery of genetic information from the fossil record as a 21st Century form of genetic time travel1. The advent of PCR made possible the amplification of small amounts of DNA from fossil samples and allowed the direct study of phylogenetics from extinct organisms. Prior to this development, phylogenetic relationships determined by genetic variation relied mostly upon sequences from living organisms. The concept of time travel, via the analysis of ancient biomolecules, can be broadened to encompass numerous types of biomolecular information recovered from ancient bones. For example, palaeodiets and palaeoclimates can be reconstructed from stable isotopes of bone collagen, and estimations of age are obtained from amino acid racemization rates.


Radiocarbon ◽  
2013 ◽  
Vol 55 (3) ◽  
pp. 1443-1453 ◽  
Author(s):  
Stuart J Fiedel ◽  
John R Southon ◽  
R E Taylor ◽  
Yaroslav V Kuzmin ◽  
Martin Street ◽  
...  

Four accelerator mass spectrometry (AMS) facilities undertook an interlaboratory exercise designed to examine the reliability and reproducibility of radiocarbon determinations on bone by dating a sample of elk (Alces alces) from Miesenheim IV. This specimen is derived from a secure geological context directly beneath the Laacher See tephra, which provides a precise terminus ante quern of ∼11,060 yr BP (∼13,050 cal yr BP). Regrettably, the results of the intercomparison exercise were complicated by evident contamination of the bone sample by exogenous organic material. This contaminant, probably humic acid, resulted in a wide span of ages (10,010 ± 30 to 11,100 ± 45 BP). The only method that yielded an accurate determination, consistent with the age of the tephra, was Oxford's single amino acid technique, which targets hydroxyproline. An acid hydrolysis step seems to have been crucial in breaking the bonds between the bone collagen and the contaminant.


2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.


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