Protein beta sheet — FTIR absorption peaks and assignments
These are the characteristic FTIR wavenumbers where Protein beta sheet tends to absorb, compiled from published literature and ranked by supporting evidence. Each assignment is traceable to a source (DOI) and cross-validated against our 130,000+ reference spectra and knowledge graph.
Backed by 8 cited sources
Quick answer
Protein beta sheet is usually assigned by looking for a recurring cluster of characteristic peaks rather than one exact textbook number. The table below shows where the literature most often places this group in FTIR, ranked by accumulated evidence.
Characteristic FTIR peaks for Protein beta sheet
| Wavenumber (cm⁻¹) | Supporting facts | Cited sources | Top confidence |
|---|---|---|---|
| 1630 | 22 | 20 | 1.0 |
| 1625 | 17 | 16 | 1.0 |
| 1624 | 13 | 12 | 1.0 |
| 1628 | 11 | 11 | 1.0 |
| 1633 | 11 | 10 | 1.0 |
| 1635 | 10 | 10 | 1.0 |
| 1620 | 9 | 8 | 1.0 |
| 1629 | 8 | 8 | 1.0 |
| 1640 | 8 | 7 | 1.0 |
| 1634 | 8 | 6 | 1.0 |
| 1693 | 7 | 7 | 1.0 |
| 1639 | 7 | 7 | 1.0 |
| 1636 | 7 | 5 | 1.0 |
| 1626 | 7 | 5 | 1.0 |
| 1632 | 6 | 6 | 1.0 |
| 1618 | 6 | 6 | 1.0 |
| 1652 | 6 | 6 | 1.0 |
| 1612 | 6 | 5 | 1.0 |
| 1623 | 6 | 4 | 1.0 |
| 1680 | 5 | 5 | 1.0 |
| 1690 | 5 | 5 | 1.0 |
| 1616 | 5 | 4 | 1.0 |
| 1650 | 5 | 4 | 1.0 |
| 1695 | 5 | 4 | 1.0 |
| 1638 | 5 | 3 | 1.0 |
| 1696 | 4 | 4 | 1.0 |
| 1637 | 4 | 4 | 0.9 |
| 1659 | 3 | 3 | 1.0 |
| 1655 | 3 | 3 | 1.0 |
| 1614 | 3 | 3 | 1.0 |
Showing the 30 best-supported peaks of 128 total for Protein beta sheet.
Possible materials
| Material | Supporting peaks | Cited sources |
|---|---|---|
| silk fibroin | 1050, 1511, 1648 | 1 |
Spectrum logic
A functional-group assignment becomes more confident when several expected bands appear together. Use this page to find the strongest-supported peaks, then confirm that the same sample exhibits a coherent pattern rather than a single isolated hit.
Real-world usage
These pages are useful for unknown material analysis, peak explanation in reports, polymer troubleshooting, and verifying whether a candidate material family is chemically plausible.
Common mistakes
- Using one functional-group page as a complete material verdict without checking the rest of the spectrum.
- Assuming the strongest band is always the most diagnostic one.
- Forgetting that processing, additives, aging, and mixtures can shift or broaden expected peaks.
Verification advice
Use DSC, GC-MS, or TGA when several material families share similar bands or when mixture effects make the FTIR assignment uncertain.
Literature behind these assignments
-
1695 cm⁻¹ confidence 1.0
“The broad bands in the raw spectrum at 1695 ad cm-1 (α-helix β-sheet 1637 were associated with amide I and cm-1 structures of proteins) while the signal at 1520 corre-”
Baldauf 等 - 2007 - Effect of selective growth media on the differenti DOI: 10.1016/j.mimet.2006.06.012 -
660 cm⁻¹ confidence 1.0
“wavenumber components of Amide I at about 1,690the 12 low-complexity, highly repetitive blocks, which are mainly 1,660cm-1, β-turns β-sheet assigned to vibrations of unordered and involved in the formation of the crystalline domains, domain”
Biagiotti 等 - 2022 - Electrospun Silk Fibroin Scaffolds for Tissue Rege DOI: 10.3389/fbioe.2022.833157 -
1614 cm⁻¹ confidence 1.0
“The line at 1614 cm-1 corresponds to the intermolecular β-sheets and 1685 cm-1”
A Preliminary Study of FTIR Spectroscopy as a Potential Non-Invasive Screening Tool for Pediatric Precursor B Lymphoblastic Leukemia DOI: 10.3390/molecules -
1618 cm⁻¹ confidence 1.0
“lower cm-1) 26 intensity of the peak (1634 corresponding to native protein structural elements such as cm-1, cm-1 cm-1) 27 β-sheets intramolecular and higher intensities of peaks (1618 1683 and 1694”
Hempseed meal protein isolates prepared by different isolation techniques. Part I. physicochemical properties DOI: 10.1016/j.foodhyd.2017.12.015 -
1550 cm⁻¹ confidence 1.0
“1550 due to bending vibration of N-H group (60%) α-helix β-sheet and stretching vibration of C-N group (40%).”
Gene-Transformation-Induced Changes in Chemical Functional Group Features and Molecular Structure Conformation in Alfalfa Plants Co-Expressing Lc-bHLH and C1-MYB Transcriptive Flavanoid Regulatory Genes: Effects of Single-Gene and Two-Gene Insertion DOI: 10.3390/ijms18030664 -
1652 cm⁻¹ confidence 1.0
“1747 β-Sheet of amide I [59-61] ](C-O) vibration ](C-N) 1652 δ(N-H),”
Hssaini 等 - 2022 - Do Pollination and Pollen Sources Affect Fig Seed DOI: 10.1155/2022/3969165 -
1668 cm⁻¹ confidence 1.0
“The the band at 1668 During the binding of Cu(II) ions, the intensity of the band at cm-1 cm-1, β-sheet R-helix, are assigned to the which is assigned to an decreased while the bands at 1620 and 1680 1650 conformation.Thevalueof1620cm-1fora”
Kim 等 - 2010 - Molecular Rearrangement of Metal-Chelating Lipid M DOI: 10.1021/la902052f -
1676 cm⁻¹ confidence 1.0
“The positive influence of PC2 loadings had three peaks at 1676, 1630 cm-1 assigned to amide I (β-turns and β-sheets), and 1063 cm-1 (mostly might be related to cellulose and hemicellulose) which differentiated the control SR (outstanding) f”
Specific Mycoparasite-Fusarium Graminearum Molecular Signatures in Germinating Seeds Disabled Fusarium Head Blight Pathogen’s Infection DOI: 10.3390/ijms22052461
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