1975
DOI: 10.1002/bip.1975.360140211
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Raman scattering of collagen, gelatin, and elastin

Abstract: SynopsisThe ltaman spectra of collagen, gelatin, and elastin are presented. The Raman lines in the latter two spectra are assigned by deuterating the amide N-H groups in gelatin and by studying the superposition spectra of the constituent amino acids. Two lines appear a t 1271 and 1248 cm-1 in the spectra of collagen and gelatin that can be assigned to the amide I11 mode. Possibly, the appearance of two amide I11 lines is related to the biphasic nature of the tropocollagen molecule, i.e., proline-rich (nonpola… Show more

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Cited by 381 publications
(332 citation statements)
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References 20 publications
(2 reference statements)
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“…Spectra from the internal surfaces of both the rock pigeon and chicken eggshells provided evidence of calcite and a matrix protein (e.g. collagen or albumin; Frushour and Koenig, 1975). Five spectral peaks attributed to protein were well resolved in analyses of the chicken eggshell (internal), and 17 protein-attributed peaks could be identified in spectra from the rock pigeon eggshell (internal).…”
Section: Identifying Other Eggshell Constituentsmentioning
confidence: 99%
“…Spectra from the internal surfaces of both the rock pigeon and chicken eggshells provided evidence of calcite and a matrix protein (e.g. collagen or albumin; Frushour and Koenig, 1975). Five spectral peaks attributed to protein were well resolved in analyses of the chicken eggshell (internal), and 17 protein-attributed peaks could be identified in spectra from the rock pigeon eggshell (internal).…”
Section: Identifying Other Eggshell Constituentsmentioning
confidence: 99%
“…Table 1 summarizes the Raman shift and the assignment of the bands, which are discussed in terms of riboflavin-UVA and collagen interactions. [26][27][28][29][30][31] Fig. 1 Raman spectra of the normal and cross-linked human sclera tissue in three spectral ranges of (a) 200 to 3200 cm − 1 , (b) 200 to 1800 cm − 1 , and (c) 2800 to 3200 cm − 1 , respectively.…”
Section: Histological Analysismentioning
confidence: 99%
“…Thus, it can provide critical data on triple helix to random coil transitions that may occur in dentin collagen as a result of heat, acid or other degrading reagents. In the Raman spectra of collagen, bands associated with amide I and III are particularly sensitive to conformational changes in the triple helix [73].…”
Section: Dentin Smear Layermentioning
confidence: 99%