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
Characteristic FTIR peaks for Protein beta sheet
| Wavenumber (cm⁻¹) | Supporting facts | Cited sources | Top confidence |
|---|---|---|---|
| 1630 | 8 | 7 | 1.0 |
| 1640 | 6 | 5 | 0.9 |
| 1635 | 4 | 4 | 1.0 |
| 1625 | 4 | 4 | 1.0 |
| 1629 | 4 | 4 | 0.9 |
| 1637 | 4 | 4 | 0.9 |
| 1626 | 4 | 3 | 0.95 |
| 1636 | 4 | 3 | 0.95 |
| 1693 | 3 | 3 | 0.9 |
| 1624 | 3 | 3 | 0.9 |
| 1633 | 3 | 2 | 0.95 |
| 1623 | 3 | 2 | 0.9 |
| 1631 | 2 | 2 | 0.95 |
| 1690 | 2 | 2 | 0.9 |
| 1628 | 2 | 2 | 0.8 |
| 1616 | 2 | 1 | 1.0 |
| 1695 | 2 | 1 | 0.9 |
| 1634 | 2 | 1 | 0.9 |
| 1638 | 2 | 1 | 0.9 |
| 1620 | 2 | 1 | 0.9 |
| 1689 | 2 | 1 | 0.9 |
| 1610 | 2 | 1 | 0.8 |
| 1656 | 1 | 1 | 1.0 |
| 1675 | 1 | 1 | 1.0 |
| 1696 | 1 | 1 | 0.95 |
| 1520 | 1 | 1 | 0.9 |
| 1691 | 1 | 1 | 0.9 |
| 1697 | 1 | 1 | 0.9 |
| 1618 | 1 | 1 | 0.9 |
| 1649 | 1 | 1 | 0.9 |
Showing the 30 best-supported peaks of 49 total for Protein beta sheet.
Literature behind these assignments
-
1625 cm⁻¹ confidence 1.0
“Text: 'peaks at 1625 (intermolecular β-sheet) and ... (β-sheet)'”
Lin 等 - 2004 - Pressure dependence of human fibrinogen correlated DOI: 10.1002/bip.20012 -
1616 cm⁻¹ confidence 1.0
“Explicitly assigned in text.”
Wu 和 Zuo - 2011 - Research on Structure and Property of Silk Fibroin DOI: 10.4028/www.scientific.net/AMR.175-176.176 -
1635 cm⁻¹ confidence 1.0
“assigned to β-sheet”
Frare 等 - 2006 - Identification of the core structure of lysozyme a DOI: 10.1016/j.jmb.2006.06.055 -
1656 cm⁻¹ confidence 1.0
“Text: 'amide I (1656 for cm-1 α-helix β-sheet)'”
Peris 等 - 2023 - Roadmap for Postnatal Brain Maturation Changes in DOI: 10.1021/acschemneuro.3c00237 -
1630 cm⁻¹ confidence 1.0
“amide I vibration characteristic of β-sheet rich secondary structures”
Sood 等 - 2011 - Disassembly of preformed amyloid beta fibrils by s DOI: 10.1016/j.bmcl.2011.02.012. -
1636 cm⁻¹ confidence 0.95
“Explicit assignment: 'β-sheet band ca. 1636 cm-1'.”
Yu 等 - 2015 - Molecular basis of processing-induced changes in p DOI: 10.1016/j.saa.2015.06.050 -
1631 cm⁻¹ confidence 0.95
“Explicit assignment: 'Amide I bands close to 1631 and 1696 are β-sheet ... indicative of secondary structure'”
Hepler 等 - 2018 - Spectroscopic analysis of chlamydial major outer m DOI: 10.1002/pro.3501 -
1626 cm⁻¹ confidence 0.95
“Explicit assignment in text.”
Komorek 等 - 2021 - Adsorption and Conformation Behavior of Lysozyme o DOI: 10.3390/ijms22031322
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