International Scholarly Research Notices / 2012 / Article / Tab 4 / Research Article
Fluorescence Rejection by Shifted Excitation Raman Difference Spectroscopy at Multiple Wavelengths for the Investigation of Biological Samples Table 4 Raman bands identified in the SERDS spectra of bone from beef and pork and their vibrational assignment, Hyp: Hydroxyproline, Pro: Proline, Phe: Phenylalanine, Tyr: Tyrosine.
Vibrational assignment 783 nm excitation 671 nm excitation 488 nm excitation Literature value [References]
𝜈
2
P
O
4
3
-
432 432 — 422–454 [37 ]
𝜈
2
P
O
4
3
-
455 451 — 422–454 [37 ] Quartz 494 494 489
𝜈
4
P
O
4
3
-
583 583 581 578–617 [37 ]
𝜈
4
P
O
4
3
-
615 612 612 578–617 [37 ] CH2 rocking 723 719 — 730 [30 ] CH2 rocking 784 781 780 779 [30 ]
𝜈
C–C of collagen backbone815 813 812 815 [38 ]
𝜈
C–C of Pro853 851 850 855-856 [35 ]
𝜈
C–C of Hyp880 884 — 871–876 [39 ]
𝜈
C–C of Pro918 912 — 920-921 [35 ]
𝜈
1
P
O
4
3
-
958 958 957 957–963 [39 ] Phe
𝜈
CC ring 1004 1002 1001 1003-1004 [38 , 40 ] Carotenoid — — 1001 1000–1014 [21 ]
𝜈
3
P
O
4
3
-
1031 1030 1026 1030–1032 [39 , 41 ]
𝜈
1
C
O
3
2
-
,
𝜈
3
P
O
4
3
-
1071 1070 1067 1065–1075 [37 , 40 ]
𝜈
(C–N)1103 1099 1101 1093–1101 [31 , 35 ]
𝜈
(C–N) of protein1128 1125 1125 1122–1125 [36 ] Carotenoid — — 1155 1151–1172 [21 ]
𝜈
CH2 ,
𝜌
CH3 1161 1160 — 1163 [30 ] Hyp, Tyr 1203 1200 1197 1202–1211 [33 , 35 ] Amide III 1243 1241 1241 1243–1320 [37 ] Amide III 1272 1269 1266 1243–1320 [37 ] Amide III 1320 1317 — 1243–1320 [37 ] CH2 wagging 1344 1341 1344 1340–1343 [31 ] CH2 deformation 1378 1375 1374 1379 [31 ]
𝛿
CH2 , scissoring1450 1448 1447 1447–1452 [37 ]
𝛿
(CH3 , CH2 )1464 1466 — 1461–1464 [32 , 33 ] Carotenoid — — 1518 1511–1535 [21 ] Phe, Tyr 1603 1599 1602 1603–1606 [32 , 36 ] Amide I
𝜈
C=O (
𝛼
-helix) 1630 1629 1629 1640–1670 [38 ] Amide I
𝜈
C=O (
𝛼
-helix) 1662 1658 1659 1640–1670 [38 ] Amide I
𝜈
C=O (
𝛼
-helix) 1683 1681 1679 1640–1670 [38 ]
