Infrared spectra database - Depository of FTIR spectra of IDAP parchments
- 3283 cm-1 : Amide A: >95% ν(NH), and 1st overtone Amide II
- 3073 cm-1: Amide B: ν(NH) and 1st overtone Amide II
- 2948 cm-1 : νas(CH3)
- 2928 cm-1 : νas(CH2)
- 2878 cm-1 : v(CH3)
- 2865 cm-1 : v(CH2)
- 1795 cm-1 : overtone of ν(CO32-) and Ca2+ of CaCO3
- 1720 cm-1 : ν(C=O) in –COOH
- 1620 cm-1 : δ(O–H) in strongly held water molecules in CaSO4.H2O (gypsum)
- 1631 cm-1 : Amide I: 80% ν(C=O) and 20% [ν(CN), δ(NH)]
- 1580 cm-1 : νas(C=O) in –COO- (Asp and Glu)
- 1536 cm-1 : Amide II: 40-60% δ(NH), and ν(CN)
- 1451 cm-1 (may be hidden by CaCO3): δ(CH2) and δ(CH3)
- 1447 cm-1 : νas(CO32-) in CaCO3
- 1401 cm-1 (may be hidden by CaCO3): ν(C=O) in –COO-
- 1338 cm-1 : Side chain vibration of collagen
- 1286 cm-1 : Amide III with δ(CH2) from glycine backbone and proline sidechain
- 1236 cm-1 : Amide III: 30% ν(CN), 30% δ(NH), ~20% ν(C-C), ~10% δ(CH)
- 1202 cm-1 : Amide III with δ(CH2) from glycine backbone and proline sidechain
- 1163 cm-1 : ν(C-O) of carbohydrates
- 1084 cm-1, 1031 cm-1 : ν(C-O) of carbohydrates and proteoglycans
- 1062 cm-1 : ν(C-O) of carbohydrates and ν(SO3-) of sulphated glycosaminoglycans
- 874 cm-1 : δ(CO32-) in CaCO3
This site contains a database depository of the Attenuated Total Reflection / Fourier Transform Infrared (ATR/FTIR) spectra of new, accelerated aged and historical/archival parchments that were collected for the IDAP project in 2005. Damage assessment was based on spectral changes in collagen, in particular within the amide I carbonyl stretching region, which is sensitive to changes in the triple helical structure of collagen. The ATR/FTIR damage assessment has been published elsewhere [1, 2].
The findings of the ATR/FTIR of these parchments are in line with damage assessment by atomic force microscopy (AFM), which monitored the eventual loss in the D-spacing of the collagen fibrils, micro-thermal analysis (micro-TA) showing enhanced transitions with increased degradation, and dynamic mechanical analysis with controlled humidity (DMA/RH) which showed that the displacement of parchment under a small strain is reduced with increased RH as a function of increased state of denaturation of collagen [1].
Considering slight shifts in the frequencies, the spectral information is listed below:
Marianne Odlyha, Thermal Analysis and Conservation Science Laboratory, Department of Biological Sciences, University of London Birkbeck College, London, UK, IDAP project partner is acknowledged for making the spectra acquired with Charis Theodorakopoulos available. Without this contribution this depository would not have been possible.
1. Odlyha, M., Theodorakopoulos, C., de Groot, J., Bozec. L. and M. Horton. Thermoanalytical (macro to nano-scale) techniques and non-invasive spectroscopic analysis for damage assessment of parchment. In: Larsen R, editor. Improved damage assessment of parchment (IDAP), Assessment, data collection and sharing of knowledge European Commission, Research Report no 18. Luxembourg: Publications Office, 2007. p. 73-85. ISBN 978-9279053788 - download
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REFERENCES
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