Protein beta sheet — Puncak serapan FTIR dan tugasan
Ini adalah nombor gelombang FTIR ciri di mana Protein beta sheet cenderung menyerap, disusun dari literatur yang diterbitkan dan disusun berdasarkan bukti sokongan. Setiap tugasan dapat dikesan ke sumber (DOI) dan disahkan silang terhadap 130,000+ spektrum rujukan dan graf pengetahuan kami.
Backed by 8 cited sources
Jawapan pantas
Protein beta sheet biasanya ditetapkan dengan mencari kelompok berulang puncak ciri dan bukan satu nombor tepat buku teks. Jadual di bawah menunjukkan di mana literatur paling kerap meletakkan kumpulan ini dalam FTIR, yang disusun mengikut bukti terkumpul.
Puncak FTIR ciri untuk Protein beta sheet
| Nombor gelombang (cm⁻¹) | Fakta sokongan | Sumber dipetik | Keyakinan tertinggi |
|---|---|---|---|
| 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 |
Menunjukkan 30 puncak terbaik disokong daripada 128 jumlah untuk Protein beta sheet.
Bahan yang mungkin
| Bahan | Puncak sokongan | Sumber dipetik |
|---|---|---|
| silk fibroin | 1050, 1511, 1648 | 1 |
Logik spektrum
Tugasan kumpulan berfungsi menjadi lebih yakin apabila beberapa jalur yang dijangkakan muncul bersama. Gunakan halaman ini untuk mencari puncak yang paling disokong, kemudian sahkan bahawa sampel yang sama menunjukkan corak yang koheren dan bukannya satu hit terpencil.
Penggunaan dunia sebenar
Halaman-halaman ini berguna untuk analisis bahan yang tidak diketahui, penjelasan puncak dalam laporan, penyelesaian masalah polimer, dan mengesahkan sama ada keluarga bahan calon adalah boleh dipercayai secara kimia.
Kesilapan biasa
- Menggunakan satu halaman kumpulan berfungsi sebagai keputusan bahan lengkap tanpa memeriksa spektrum yang lain.
- Dengan menganggap jalur yang paling kuat sentiasa menjadi yang paling diagnostik.
- Melupakan bahawa pemprosesan, bahan tambahan, penuaan, dan campuran boleh mengalihkan atau melebarkan puncak yang dijangkakan.
Nasihat pengesahan
Gunakan DSC, GC-MS, atau TGA apabila beberapa keluarga bahan berkongsi jalur yang serupa atau apabila kesan campuran menyebabkan tugasan FTIR tidak pasti.
Literatur di sebalik penetapan ini
-
1695 cm⁻¹ keyakinan 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 keyakinan 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 keyakinan 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 keyakinan 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 keyakinan 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 keyakinan 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 keyakinan 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 keyakinan 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
Lihat Protein beta sheet dalam spektrum anda sendiri
Muat naik spektrum FTIR anda dan dapatkan laporan tafsiran penuh — tugasan puncak dengan petikan literatur, padanan perpustakaan, dan analisis berasaskan literatur — dalam beberapa saat.