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Assessing the extent of bone degradation using glutamine deamidation in collagen

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Assessing the extent of bone degradation using glutamine deamidation in collagen. / Wilson, Julie; van Doorn, Nienke L; Collins, Matthew J.

In: Analytical Chemistry, Vol. 84, No. 21, 06.11.2012, p. 9041-9048.

Research output: Contribution to journalArticlepeer-review

Harvard

Wilson, J, van Doorn, NL & Collins, MJ 2012, 'Assessing the extent of bone degradation using glutamine deamidation in collagen', Analytical Chemistry, vol. 84, no. 21, pp. 9041-9048. https://doi.org/10.1021/ac301333t

APA

Wilson, J., van Doorn, N. L., & Collins, M. J. (2012). Assessing the extent of bone degradation using glutamine deamidation in collagen. Analytical Chemistry, 84(21), 9041-9048. https://doi.org/10.1021/ac301333t

Vancouver

Wilson J, van Doorn NL, Collins MJ. Assessing the extent of bone degradation using glutamine deamidation in collagen. Analytical Chemistry. 2012 Nov 6;84(21):9041-9048. https://doi.org/10.1021/ac301333t

Author

Wilson, Julie ; van Doorn, Nienke L ; Collins, Matthew J. / Assessing the extent of bone degradation using glutamine deamidation in collagen. In: Analytical Chemistry. 2012 ; Vol. 84, No. 21. pp. 9041-9048.

Bibtex - Download

@article{99902de4750448f59b3cb3cf961afd81,
title = "Assessing the extent of bone degradation using glutamine deamidation in collagen",
abstract = "Collagen peptides are analyzed using a low-cost, high-throughput method for assessing deamidation using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). For each chosen peptide, the theoretical distribution is calculated and the measured distribution for each sample compared with this to determine the extent of glutamine deamidation. The deamidation of glutamine (Q) to glutamic acid (E) results in a mass shift of +0.984 Da. Thus, from the resolution of our data, the second peak in the isotope distribution for a peptide containing one glutamine residue coincides with the first peak of the isotope distribution for the peptide in which the residue is deamidated. A genetic algorithm is used to determine the extent of deamidation that gives the best fit to the measured distribution. The method can be extended to peptides containing more than one glutamine residue. The extent of protein degradation assessed in this way could be used, for example, to assess the damage of collagen, and screen samples for radiocarbon dating and DNA analysis.",
author = "Julie Wilson and {van Doorn}, {Nienke L} and Collins, {Matthew J}",
year = "2012",
month = nov,
day = "6",
doi = "10.1021/ac301333t",
language = "English",
volume = "84",
pages = "9041--9048",
journal = "Analytical Chemistry",
issn = "0003-2700",
publisher = "American Chemical Society",
number = "21",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Assessing the extent of bone degradation using glutamine deamidation in collagen

AU - Wilson, Julie

AU - van Doorn, Nienke L

AU - Collins, Matthew J

PY - 2012/11/6

Y1 - 2012/11/6

N2 - Collagen peptides are analyzed using a low-cost, high-throughput method for assessing deamidation using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). For each chosen peptide, the theoretical distribution is calculated and the measured distribution for each sample compared with this to determine the extent of glutamine deamidation. The deamidation of glutamine (Q) to glutamic acid (E) results in a mass shift of +0.984 Da. Thus, from the resolution of our data, the second peak in the isotope distribution for a peptide containing one glutamine residue coincides with the first peak of the isotope distribution for the peptide in which the residue is deamidated. A genetic algorithm is used to determine the extent of deamidation that gives the best fit to the measured distribution. The method can be extended to peptides containing more than one glutamine residue. The extent of protein degradation assessed in this way could be used, for example, to assess the damage of collagen, and screen samples for radiocarbon dating and DNA analysis.

AB - Collagen peptides are analyzed using a low-cost, high-throughput method for assessing deamidation using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). For each chosen peptide, the theoretical distribution is calculated and the measured distribution for each sample compared with this to determine the extent of glutamine deamidation. The deamidation of glutamine (Q) to glutamic acid (E) results in a mass shift of +0.984 Da. Thus, from the resolution of our data, the second peak in the isotope distribution for a peptide containing one glutamine residue coincides with the first peak of the isotope distribution for the peptide in which the residue is deamidated. A genetic algorithm is used to determine the extent of deamidation that gives the best fit to the measured distribution. The method can be extended to peptides containing more than one glutamine residue. The extent of protein degradation assessed in this way could be used, for example, to assess the damage of collagen, and screen samples for radiocarbon dating and DNA analysis.

UR - http://www.scopus.com/inward/record.url?scp=84868568537&partnerID=8YFLogxK

U2 - 10.1021/ac301333t

DO - 10.1021/ac301333t

M3 - Article

C2 - 23030643

VL - 84

SP - 9041

EP - 9048

JO - Analytical Chemistry

JF - Analytical Chemistry

SN - 0003-2700

IS - 21

ER -