International Scholarly Research Notices

Research Article

Fluorescence Rejection by Shifted Excitation Raman Difference Spectroscopy at Multiple Wavelengths for the Investigation of Biological Samples

Table 3

Raman bands identified in the SERDS spectra of connective tissue from beef and pork and their vibrational assignment, Hyp: Hydroxyproline, Pro: Proline, Phe: Phenylalanine, Trp: Tryptophan, Tyr: Tyrosine.
Vibrational assignment783 nm excitation671 nm excitation488 nm excitationLiterature value
[References]
Quartz492494489 
Quartz602602602  
CH2 rocking721723—730 [30]
Trp ring breathing757757753756 [30]
CH2 rocking782781783779 [30]
𝜈 (C–O–C); 𝜈 (C–C) of backbone814813817812–821 [31–33]
𝜈 (C–C) of Pro ring853853852852–860 [32, 33]
𝜈 (C–C) of Hyp ring875875873873–884 [31, 34]
𝜈 (C–C) of Pro ring918919919920–925 [32, 33]
𝜈 (C–C) of protein backbone939938937936–938 [32, 33]
Carotenoid——963960–965 [20]
𝜈 (C–C) of residue970969—957–961 [30, 31]
Phe1002100210021003–1006 [32, 33]
Carotenoid——10021000–1014 [21]
Phe, Pro10311032—1032–1037 [31, 33]
Bend of carboxyl OH10601058—1062–1065 [31]
𝜈 (C–N)11001099—1093–1101 [31, 35]
𝜈 (C–N) of protein1126112511241122–1125 [36]
Carotenoid——11541151–1172 [21]
𝜈 CH2, 𝜌 CH311591162—1163 [30]
Carotenoid——11881191–1193 [20]
Hyp, Tyr12031202—1202-1211 [33, 35]
Carotenoid——12111213–1215 [20]
Amide III1240124012431239–1248 [32, 33]
Amide III1271127312701263–1273 [30, 33]
CH2 twisting1318131713141314–1319 [31, 33]
CH2 wagging1342134113401340–1343 [31]
CH2 deformation1378137713741379 [31]
𝜈 s (COO-)1424142414231416–1427 [32, 35]
𝛿 (CH3, CH2)1450144814481447–1452 [32, 33, 36]
𝛿 (CH3, CH2)1461146414681461–1464 [32, 33]
Carotenoid——15211511–1535 [21]
Phe, Tyr1603159915981603–1606 [32, 36]
Amide I16301629—1636–1642 [32, 33]
Amide I1662166016581650–1680 [30]