International Scholarly Research Notices

Research Article

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

Table 1

Raman bands identified in the SERDS spectra of meat from beef and pork and their vibrational assignment, Phe: Phenylalanine, Trp: Tryptophan, Tyr: Tyrosine.
Vibrational assignment783 nm excitation671 nm excitation488 nm excitationLiterature value
[References]
Quartz492492489 
Quartz603602602 
Myoglobin——671671–678 [13, 14]
Adenine720717—720 [15]
Trp757753752750–760 [16, 17]
Quartz782783780
Tyr 𝜈 -ring827825826827–834 [15, 16, 18]
Tyr 𝜈 -ring855853852850–860 [16]
Trp 𝜈 -ring880875—877–881 [15, 16]
𝜈 C–C901902—900–901 [16, 19]
𝜈 C–C936935937934–944 [16]
Carotenoid——960960–965 [20]
Phe 𝜈 -ring1002100210011000–1006 [16, 17]
Carotenoid——10021000–1014 [21]
C–C ring bend (Phe)10331032—1030–1033 [17, 19]
𝜈 C–N, 𝜈 C–C10471049—1040–1120 [19]
𝜈 C–N, 𝜈 C–C1081107710761040–1120 [19]
𝜈 C–N1126112511251127–1130 [18, 22]
𝜈 C–C, 𝛿 COH11561154—1156 [15]
Carotenoid——11541151–1172 [21]
Tyr11731171—1172–1175 [15, 22]
Carotenoid——11881191–1193 [20]
Tyr, Phe12061203—1205–1209 [17, 19]
Carotenoid——12101213–1215 [20]
Amide III ( 𝛽 -chain, random)12421234—1225–1250 [19]
Amide III ( 𝛼 -helix)12661266—1265–1278 [17, 19]
Amide III ( 𝛼 -helix)13041304—1301–1309 [15, 16]
Trp; δCH13411339—1339–1342 [15, 16, 19]
Myoglobin——13511353–1371 [13, 14]
𝛿 CH31395139413971395 [15]
𝛿 a s CH3, 𝛿 CH2, 𝛿 CH1447144614471447–1451 [17, 19]
CH2 and CH3 bending1460146114651460–1483 [16]
Carotenoid——15201511–1535 [21]
Trp 𝜈 -ring15501549—1553-1554 [16]
Trp, Phe, Tyr 𝜈 -ring1603161016011605–1618 [15, 16]
Amide I ( 𝛼 -helix)1648164716531645–1658 [16, 18]