Protein alpha helix — Puncak serapan FTIR dan tugasan

Jawapan pantas

Protein alpha helix 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 alpha helix

Menunjukkan 30 puncak terbaik disokong daripada 97 jumlah untuk Protein alpha helix.

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
• 1648 cm⁻¹ keyakinan 1.0

  “cm-1 The vibration 1648 is assigned to C=O stretching of amide I in proteins (mainly - A helix components of proteins) [24, 31].”

  Fourier transform infrared microspectroscopy detects biochemical changes during C. elegans lifespan DOI: 10.1016/j.vibspec.2019.04.005
• 1645 cm⁻¹ keyakinan 1.0

  “1538 0.066 1537 0.064 Amide II due to N-H bending of proteins [15,17] Amide I due to C=O stretching of α-helix proteins 1645 0.07 1641 0.071 [17] 2924 0.028 2926 0.02 asymmetric stretching symmetric CH2: lipids [18] 2965 0.027 2962 0.019 as”

  A Preliminary Study of FTIR Spectroscopy as a Potential Non-Invasive Screening Tool for Pediatric Precursor B Lymphoblastic Leukemia DOI: 10.3390/molecules
• 1650 cm⁻¹ keyakinan 1.0

  “The amide I peak (1650 cm-1) is stronger in normal tissues due to the high amount of protein with an α-helical secondary structure.”

  Ghassemi 等 - 2021 - Diagnosis of normal and malignant human gastric ti DOI: 10.1016/j.molstruc.2020.129493
• 1283 cm⁻¹ keyakinan 1.0

  “At lower wavenumber, the bands at cm-1 α-helices 1283 is assigned to of the amide III absorption band owing to in-phase combination of CH stretching and NH bending vibrations [42].”

  Gupta 等 - 2022 - In vitro cell composition identification of wood d DOI: 10.1098/rsos.201935
• 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
• 1424 cm⁻¹ keyakinan 1.0

  “in combination with a visible alteration in the protein 1049.1 and 1158.1 to 1161.5 In Muchmore, cm-1 (α-helix β-sheet) region turned to following pathogenic the peaks at 1423.5, 1375.9, and 1052.5 were cm-1”

  Synchrotron based phase contrast X-ray imaging combined with FTIR spectroscopy reveals structural and biomolecular differences in spikelets play a significant role in resistance to Fusarium in wheat DOI: 10.1186/s12870-014-0357-5
• 1655 cm⁻¹ keyakinan 1.0

  “Typically, a shoulder at is assigned to β-sheet cm-1 secondary structures of proteins, while the band at 1655 is assigned to α-helix secondary structure [24], thus amide I band of the SC at the latter frequency reflects the”

  Mansour 等 - 2017 - Elucidation of penetration enhancement mechanism o DOI: 10.1016/j.saa.2017.05.026