JOURNAL OF RAMAN SPECTROSCOPY

J. Raman Spectrosc. 2004; 35: 754–760

Published online in Wiley InterScience (www.interscience.wiley.com). DOI: 10.1002/jrs.1155

Application of Fourier transform Raman spectroscopy

to the characterization of parchment and vellum.
II — Effect of biodeterioration and chemical
deterioration on spectral interpretation
Howell G. M. Edwards1∗ and Fernando Rull Perez2
1
Department of Chemical and Forensic Sciences, University of Bradford, Bradford BD7 1DP, UK
2
Cristalografia y Mineralogia, Facultad de Ciencias, Universidad de Valladolid, Prado de la Magdalena S/N, 47011 Valladolid, Spain

Received 5 September 2003; Accepted 15 October 2003

Raman spectra of ancient parchment and vellum were recorded and used to characterize materials used
in early mediaeval (10th century) and later works. These studies support work on the characterization
of pigments used on historiated manuscripts and provide the basis for future studies of the interaction
between pigments, binders and parchment or vellum. Examination of the undecorated parts of manuscripts
or books has been undertaken to ascertain if there are traces remaining of the procedures used to prepare
the materials; in several cases, there is spectroscopic evidence for the presence of sulfates and slaked lime,
which were used in the preparation of vellums for scriptoria. The deterioration of vellums and parchments
has been related to spectroscopic observation of changes in the protein — CONH — structures and to the
chemical destruction of the — CSSC — bonds of cysteine. Band broadening resulting from the chemical
reactions at these sites was analysed. Copyright  2004 John Wiley & Sons, Ltd.

KEYWORDS: vellum; parchment; protein deterioration; exogenous materials in skin

INTRODUCTION and hydrolytic cleavage of the peptide backbone;3 a hidden

Parchment is derived from untanned animal skins from
sheep or goats; vellum is of finer quality and made from
the skins of kids, lambs, pigs and calves. These were used
as writing materials from about 200 BC until late mediaeval
times, when they were supplanted by paper. The preparation
of parchment or vellum involved the cleaning and removal of
hair mechanically by scraping the skin. This was followed by
desiccation of the skin using sodium or potassium chloride,
adjustment of the pH by treatment with ammonium chloride
or sulfate with lime and a fluid application of potash alum
with flour and egg yolk to give a final suppleness to the skin
in preparation for the artistic decoration or literary work.1
The chemical composition of parchment or vellum is
collagen, a natural biopolymer with relative molecular mass
of 350 kDa; the collagen is constructed from a triple ˛-
helix with random coil telopeptides.2 Degradation of ancient
parchment or vellum is a complex process which involves
the chemical oxidative deterioration of the amino acid chains
Ł Correspondence to: Howell G. M. Edwards, Department of
Chemical and Forensic Sciences, University of Bradford, Bradford
BD7 1DP, UK. E-mail: h.g.m.edwards@bradford.ac.uk
event in this deteriorative cycle is the conformational change
from helical to ˇ-sheet or ˇ-turn structures. Bacteriological
changes are superimposed on the chemical changes outlined
above and, in particular, target the C—S—S—C disulfide
bridges in cysteine residues, which have characteristic
conformational signatures4 near 500 cm
1 in the Raman
spectrum (Fig. 1). Physical damage also evident in ancient
parchments and vellums results in tears and holes (lacunae)
from careless or frequent handling and from digestion by
insects or grubs. Chemicals produced by lichen colonization
of parchment or vellum can result in further deterioration.5,6
Finally, changes in environmental conditions, particularly in
the humidity and in air pollution resulting from exposure
to atmospheric sulfur and nitrogen oxides from fossil fuel
combustion, can induce chemical changes within the residues
remaining from the preparation and treatment of the animal
skins, e.g. sulfur dioxide and carbon dioxide react with
hydrated lime or calcium hydroxide residues to produce
calcium sulfate and calcium carbonate, respectively.7,8
To date, most Raman spectroscopic studies of manus-
cripts7 – 11 have concentrated on the analysis of the pigments
and decoration; this has provided novel information about

Copyright  2004 John Wiley & Sons, Ltd.


' '
Figure 1. Conformational structures of the disulfide bond in
proteins based on intersecting planes containing the —C—
C—S—S—C—C— group in trans and gauche combinations.
Here, the planes indicate the relative spatial conformations of
the SS and SC groups, along with the component Newman
projections.
the techniques used in their creation. However, the state of
preservation of the substrate parchment, vellum or paper
has largely been ignored. A major reason for this can
probably be ascribed to the fluorescence emission gen-
erated from the ancient biomaterials, for which Raman
spectra recorded using 1064 nm excitation in the near-
infrared vegion is necessary for the observation of vibra-
tional features. Another major problem for the spectro-
scopic characterization of ancient vellum and parchment
is the spectral band broadening observed with protein
degradation.12,13
Copyright  2004 John Wiley & Sons, Ltd.
FT-Raman characterization of parchment and vellum 755
The availability of some badly deteriorated or damaged
parchments and vellums of low commercial value and
the viability of Raman spectroscopy for the vibrational
characterization of both organic and inorganic materials
make the study of parchment deterioration a realistic
possibility; the results could provide specific knowledge
about the material degradation which should be of direct
relevance to the preservation of parchments or vellums
which are less badly affected and which are in need of
urgent conservation procedures to prevent further damage
in archival collections.
EXPERIMENTAL
Specimens
The specimens were as follows:
1. Two fragments of vellum3 from the scriptorium of the
monastery of Santa Domingo de Silos, Spain, dating from
the 10th and 11th centuries (Plate 1).
2. Several fragments of mediaeval manuscripts from a
monastery at Puentedura, Burgos, Spain and the Biblioteca
de Universidad de Valladolid, Spain. These are all
excellent examples of important large manuscripts called
cantorals or song books and date from the 14th and 15th
centuries.
3. Specimens of modern animal skins such as pig (parch-
ment) and goat (vellum).
Raman spectroscopy
Fourier transform (FT) Raman spectra were recorded using a
Bruker IFS 66/FRA 106 instrument with Nd: YAG excitation
at 1064 nm and maximum nominal power of 100 mW.
Sample preparation was minimal since the purpose of this
study was to evaluate degradation; light swabbing of the
specimen with ethanol was undertaken to remove surface
dust and grease stains. Spectral data were recorded over
2000 accumulated scans with 8 cm
1 spectral resolution to
provide good signal-to-noise ratios from the samples. Most
of the spectroscopic features of the degraded specimens were
correct in wavenumber to better than š1 cm
1 , but severe
spectral broadening resulted in diffuse, weak bands often
on larger emission backgrounds, and in this case only band
centres were reported.
RESULTS AND DISCUSSION
Major advantages of Raman and infrared spectroscopic
techniques for the assessment of degradation of biological
specimens are the sensitivity of the analytical probe to the
conformation of proteins, to changes in hydrogen bonding
of peptide and organic sulfide groups and to the monitoring
of inorganic or mineral deposits associated with the organic
components. The last point is expressly favoured by the
Raman technique because the spectral range from about 100
J. Raman Spectrosc. 2004; 35: 754–760
756 H. G. M. Edwards and F. Rull Perez
to 3500 cm
1 can be covered in one experiment, and with
FT techniques in one spectral scan; thereby, one can obtain
analytical information simultaneously about metallo-organic
species, inorganic minerals and organic moieties. This has
been demonstrated very effectively in Raman spectroscopic
applications to archaeological materials such as ivory,14,15
resins16,17 and bone,18 which are commonly found in
excavations and for which degradation in the environment
is all too often prevalent. Hence the embrittlement of
archaeological ivories by the leaching out or destruction of
the collagen in the hydroxyapatite matrix has been studied,19
as have human teeth of similar composition.20
In a recent study,21 we endeavoured to ascertain the
stability of several natural keratotic materials to a cold
desert, desiccative environment and the results indicated
that collagenic materials behaved in a different way spectro-
scopically with regard to their proteinaceous deterioration.
A 1000-year-old mummified Adelie penguin from Antarc-
tica provided specimens of skin, fur, nail and bone for
Raman spectroscopic analysis. It transpired that the nail was
significantly better preserved than the other keratotic ana-
logues under these conditions. Similarly, generic comments
about the extent of skin survival have been made which
subsequently have not been confirmed spectroscopically; in
the case of the Alpine Ice-man, for example, the collagen
peptides have undergone extensive and significant change
from ˛-helical to ˇ-sheet and random coil conformations
which belie the description of the skin as ‘remarkably well
preserved’.22
In this way, the condition or otherwise of a parchment or
vellum mediaeval manuscript can now be given a scientific
basis for evaluation; this is vitally important for future
archival conservation projects, in which manuscripts can
be targeted for emergency recovery when evidence of the
protein breakdown is observed spectroscopically.
Table 1 gives a listing of the band wavenumbers and
molecular vibrations associated with the —CONH— bond
and nearby groups such as —CH2 — in the collagen
chain. Wavenumber shifts in the amide I band, which
is predominantly
(C O) stretching, are attributable to
secondary structural changes in the proteins, and as such
are key molecular biomarkers for the initial stages of
biodegradation.
The peptide group (—CONH—) is the most character-
istic spectroscopic functionality within a protein. The group
Table 1. Band wavenumbers (em
1 ) and molecular vibrations
associated with the —CONH group in proteins
ˇ-Pleated Random
˛-Helix sheet coil
Amide I 1660–1645 1680–1665 1670–1660
Amide II 1310–1260 1240–1225 1260–1240
Skeletal C–C 950–885 1010–1000 960–950
Copyright  2004 John Wiley & Sons, Ltd.
is considered to be structurally planar, ascribed to bond
resonance stabilization; the distinctive vibrational features
are the amide I, II, III, IV, V, VI, VII, A and B bands. With
the operation of vibrational spectroscopic selection rules, the
amide I, II, III, A and B bands are infrared active, whereas
the amide I, III, A and B bands are Raman active;2 the amide
I and III bands are depicted in Fig. 1. The amide I band
arises mainly from the C O stretching vibration with a
small contribution from N–H in-plane bending. The amide
III band arises from a combination of N–H bending and
C–N stretching. The amide A and B bands both originate
from a Fermi resonance between the first excited state of the
N–H stretching vibration and the overtone of the amide II
vibration.
The amide I, II and III bands are conformationally
sensitive and can be used to identify the type of protein
secondary structure (Table 1); the wavenumber positions
of these amide bands are characteristic of secondary
structures, especially when used in conjunction with the
C–C skeletal vibrations.2 Other characteristic vibrations of
protein aminoacids are those originating from the CH2 and
CH3 groups and the C–H and C–C aromatic ring vibrations
of aromatic rings in phenylalanine, tyrosine and tryptophan.
Cystine is an important amino acid in which oxidation
of the thiol group results in a disulfide cross link bond
formation between two cystine residues and a stabilization
of the protein structures; the —S—S— bond is inactive
in the infrared but has characteristic Raman wavenumbers
dependent on the conformational arrangement between
the —C—C—S—S—C—C— moiety in the cross-linkage.
The Raman bands for different conformations of the S–S
stretching mode occur in the range 490–530 cm
1 and some
of these conformations are depicted in Fig. 2.
Figure 3 shows the Raman spectrum of natural type 1
collagen, which exhibits the characteristic protein features
discussed above, with a prominent ˛-helical amide I mode
at 1665 cm
1 , an N–H deformation mode at 1449 cm
1 and
a C–H, N–H deformation mode at 1245 cm
1 . A sharp,
symmetric ring stretching mode arising from phenylalanine
is at 1004 cm
1 . In contrast, the Raman spectra of modern
parchment and vellum are shown for the CH stretching and
protein functionality regions in Figs 4 and 5, respectively.
Several important conclusions for the analytical capability
of FT-Raman spectroscopy in parchment and vellum char-
acterization are evident from a comparison between Figs 3,
4 and 5. There is no evidence for the presence of NH and
Figure 2. Characteristic molecular vibrations of the amide I and
III modes with Raman activity.
J. Raman Spectrosc. 2004; 35: 754–760
 FT-Raman characterization of parchment and vellum

Plate 1. Mediaeval vellum specimens with script in cinnabar.

Copyright  2004 John Wiley & Sons, Ltd. J. Raman Spectrosc. 2004; 35

Figure 3. FT-Raman spectrum of collagen. Excitation
wavelength 1064 nm, wavenumber range 50–3600 cm
1 ,
1000 scans at 4 cm
1 spectral resolution.
Figure 4. FT-Raman spectra stackplot of (top) modern
parchment (pigskin) and (bottom) modern vellum (kidskin).
Excitation wavelength 1064 nm, 4 cm
1 spectral resolution,
2000 scans, wavenumber region 2750–3250 cm
1 .
OH modes in the higher wavenumber region, so the extent
of desiccation of the skin substrate in a manuscript can-
not be assessed here. Second, the protein amide stretching
and bending modes in the skin specimens have clearly sig-
nificantly broader bandwidths compared with the keratotic
collagen. This is a consequence of the natural composition
of the complex skin protein structures in terms of ˛-helix,
ˇ-sheet, ˇ-turn and random coil conformations, as well as
the presence of variable quantities of lipid in the skin protein
matrix. In particular, the loss of spectral definition in the
1200–1350 cm
1 region and the smaller band intensity of
the symmetric ring stretching (breathing) mode at 1004 cm
1
should be noted. Table 2 gives a wavenumber listing and an
approximate vibrational assignment for modern parchment
and vellum ‘control’ specimens.
Copyright  2004 John Wiley & Sons, Ltd.
FT-Raman characterization of parchment and vellum 757
Figure 5. FT-Raman spectra of modern parchment and vellum
specimens. Conditions as in Fig. 4, but wavenumber region
900–1800 cm
1 .
Figure 6. FT-Raman spectra of two regions of bleached
mediaeval vellums in a ‘good’ state of preservation, for which
the amide vibrations are well- defined.
Figures 6 and 7 show the FT-Raman spectra of the ancient
mediaeval parchment and vellum specimens in which the
protein structures show evidence of deterioration to different
extents. For example, the two spectra in Fig. 6 indicate that
the major amide I and III features of the protein groups
are present but there is no trace at all remaining of the
sulfur–sulfur cross-linkage near 500 cm
1 . The medium-
intensity broad band centred at 770 cm
1 is evidence of the
lime treatment to which the parchment has been subjected
during its preparation for manuscript usage. The presence
of weak bands at 712 and 1086 cm
1 in the upper spectrum
is indicative of a conversion to calcite occurring; from the
low intensity of these bands we can conclude that the skin is
desiccated as moisture is required23 to effect the reaction of
calcium oxide/hydroxide to calcium carbonate by absorption
of atmospheric carbon dioxide. The lower spectrum in Fig. 6
J. Raman Spectrosc. 2004; 35: 754–760
758 H. G. M. Edwards and F. Rull Perez

Table 2. Vibrational wavenumbers (cm
1 ) and assignments for

modem parchment and vellum

Wavenumber cm
1
Approximate description
Parchment Vellum of vibrational mode

3059 w 3060 w
(CH) olefinic

— —
CH aromatic
2975 w, sh 2988 w

2970 w
CH3  asymmetric
2931 s
CH3  asymmetric
2900 w
CH2 
2883 w 2880 m
CH2  asymmetric
2852 m 2850 m
CH2  asymmetric
Figure 7. FT-Raman spectra of two regions of bleached
1670 vw, sh —
C O amide I ˇ-sheet
mediaeval vellums, wavenumber region 50–1800 cm
1 . The
1652 s 1656 s
C O amide I ˛-helix
absence of the SS and CS modes is indicative of the onset of
1610 w, br 1612 w, br
C C olefinic
deterioration of the protein substrate. The broad band centred
1584 w —
C C olefinic
at 770 cm
1 in each spectrum is indicative of the lime
1554 vw 1555 mw
CN and υNH amide II
treatment to which the skin had been subjected in the
1460 w, sh 1460 w, sh υCH2 
preparation process for the manuscript.
1445 s, br 1446 s, br υCH2  scissoring
— 1421 w υCH3 
1340 mw, br 1342 mw υCH3  which it can be concluded that the substrate of the manuscript
1336 m 1338 m υCH2  has regions which differ in water content.
1299 w, br 1295 w, br CCH2  twisting Figure 7, which shows three spectra from other regions
1276 mw 1275 mw
CN and υNH amide III of the mediaeval manuscripts, reveals a different result; here,
1208 mw
CC ring the protein features are now very broad, reflecting significant
1172 w 1172 w
CC change in conformations from the predominantly ˛-helical
1156 w 1155 w
CC; υCOH structures expected for the modern analogues. Significant
1126 mw 1126 mw
CC skeletal, trans proportions of random coil and ˇ-sheet structures are now
conformation evident in these regions. Again, the S–S modes are absent. It is
1084 w, br 1084 w, br
CC skeletal, random realistic to conclude, therefore, that for all cases studied here,
conformation the primary deteriorative indicator of substrate change in
1062 w 1062 w
CC skeletal, trans ancient manuscripts is the disappearance of the C—S—S—C
conformation cross-links, which occurs even when the amide secondary
1030 mw 1030 mw
CC skeletal, cis and tertiary structures are still reasonably well preserved.
conformation It is now possible to propose some molecular structural
1002 m 1002 m
CC aromatic ring, conclusions from comparisons of Figs 3–7, namely:
phenylalanine ž The bands in the collagen are sharp and well defined:
960 w 960 w CH3 ; υCH olefinic the
(S–S) mode indicates a preferred trans–trans–gauche
934 w, br 930 w CH3  terminal;
CC˛-helix conformation. In the ancient parchment spectra the bands
891 mw 887 w CH2  are absent altogether, which reflects the destruction of
850 w 850 w υCCH aromatic the S—S bonds. This has a serious implication for the
828 w 828 w υCCH aliphatic conservation of manuscripts for which the deterioration is
743 w 740 w CH2  in-phase not observable visually.
643 mw 642 w
CS; amide IV ž The amide I band at 1667 cm
1 is characteristic of an
620 mw 620 w
CS; ˛-helical structure: the broadening of this band towards
— — CH wagging lower wavenumbers is attributable to a structural change
towards a ˇ-sheet/random coil configuration.
524 m 520 mw
SS ž New bands appear in the degraded vellum spectrum: in
417 w 420 w υCCC skeletal backbone particular a broad feature centred at 770 cm
1 assignable
to a ‘limewash’ composition of calcium oxide and calcium
hydroxide remaining from the skin preparation process.
was obtained from a different part of the manuscript and ž Carbon dioxide is believed to react with the calcium
this shows barely any evidence for calcium carbonate, from hydroxide in the prepared parchment to produce calcium

Copyright  2004 John Wiley & Sons, Ltd. J. Raman Spectrosc. 2004; 35: 754–760
 FT-Raman characterization of parchment and vellum 759

carbonate with main features at 1086, 712 and 281 cm
1 .
All of these are present as bands in the spectrum
of ancient vellum in Fig. 1. Atmospheric pollution by
sulfur and nitrogen oxides results in some interesting
by-products which can possibly also be identified; for
example, gypsum (calcium sulfate dihydrate) is found
from the reaction of calcite with SO2 . Unfortunately, this
cannot be uniquely identified because the
1 mode of
calcium sulfate dihydrate is at 1007 cm
1 and this is
accidentally almost degenerate in wavenumber position
to the phenylalanine ring stretching mode at 1004 cm
1 .
However, other spectral signatures of gypsum, weak but
clearly present, indicate that some degradation due to
SO2 attack on calcium carbonate has occurred in these
specimens of ancient substrate, namely, bands at 1161 and
619 cm
1 . A supportive weak feature due to the reaction
intermediate HSO4
is found at 1044 cm
1 , and this can
also be seen in degraded vellums. There is also some
chemical evidence that nitroxide radicals are formed at
peptide bonds by reaction with sulfur dioxide and one
might also expect to see a broadening of the amide I
band to reflect this. This latter effect is compromised
spectroscopically by the conformational protein changes
occurring in the same region.
Table 3 summarizes the inorganic and protein changes
resulting from the degradation of ancient parchments
or vellums through biological, chemical or atmospheric
agencies. The accumulation of the inorganic products of
deterioration in the skin substrate is akin to the treatment of
human skin in the mummification processes practised by the
ancient Egyptian civilisation, where Raman spectroscopy has
been successfully applied to the identification of exogenous
chemicals and inorganic residues in the mummified skin of
XIIth Dynasty burials.24
Although Raman spectroscopy has been a very effective
analytical technique for the characterization of organic or
mineral pigments on ancient documents, little work has
been carried out to date on the interaction between the
pigment and the organic substrate. The Raman spectrum of
the vellum fragment shown in Fig. 8 contains bands arising
from the red pigment cinnabar, mercury(II) sulfide, used
for the Latin script; these features are clearly seen at 154,
286 and 343 cm
1 in the low-wavenumber region of the
spectrum. In addition, however, the Raman spectrum of
the protein substrate is observed as the very broad ‘triplet’
feature between 1250 and 1700 cm
1 ; the most significant
conclusion that can be drawn here is that the vellum substrate
is significantly degraded, despite the presence of the applied
cinnabar, which might have been expected to have acted
as an antimicrobial or bactericidal agent. The presence of
‘limewash’ residues in the spectra with the broad feature
from calcium oxide/hydroxide centred on 770 cm
1 is also
noted, and again, a surprising point to be recognized here is
the absence of calcium carbonate bands, found elsewhere on
the unpigmented vellum. It can be surmised, therefore, that
the presence of the applied mineral pigment has protected the
vellum substrate from atmospheric attack by sulfur dioxide
and carbon dioxide but, despite this, the vellum has suffered
deterioration, probably through a chemical agent in this
case, since it could be argued that the cinnabar might have
been expected to have prevented bacterial attack on the skin
substrate.

Table 3. Inorganic and mineral feature and peaks of reactions at peptide

bonds

Inorganic and mineral features (cm
1 ) arising from skin preparation

and treatment for manuscripts

1085 s 
712 m CaCO3 (calcite)
285 ms
1145 mw 
1007 s CaSO4 Ð 2H2 O (gypsum)
667 mw
1032 mw HCO3

1045 mw HSO4

Peaks cm
1  characteristic of reactions at peptide bonds

1412–1420 mw Carboxylate, RCO2
, from reaction of atmospheric

CO2 with —CONH groups

1696 m Amide I 

 Compatible with ˛-helical to random coil

 conformational changes

1218 m Amide III

Copyright  2004 John Wiley & Sons, Ltd. J. Raman Spectrosc. 2004; 35: 754–760
760 H. G. M. Edwards and F. Rull Perez
Figure 8. FT-Raman spectrum of an unpigmented vellum leaf,
clearly showing in addition to the degraded collagen features
the presence of cinnabar (characteristic bands at 254, 286 and
343 cm
1 ) under the microscope. Wavenumber range
50–1800 cm
1 , 2000 scans, 4 cm
1 spectral resolution.
The ability to analyse the state of biomaterials in the
vicinity of applied surface coatings can be attractive and
interesting adjunct for Raman spectroscopic analysis of the
integrity of ancient artwork, and could be applied to the
following systems:
1. the preservation of painted miniatures on ivory or bone,
particularly where a state of desiccation may have resulted
in a movement of mineral deposits within the substrate to
the surface with deleterious effect on the artwork;
2. the assessment of the extent of biodeterioration or
chemical deterioration of fabrics (silks, cotton, linens)
and woven goods such as canvas;
3. the effect of retouching or restoration of ancient paper,
vellums and parchments.
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J. Raman Spectrosc. 2004; 35: 754–760