Protein random coil — FTIR absorption peaks and assignments
These are the characteristic FTIR wavenumbers where Protein random coil 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 random coil
Letteratura dietro queste assegnazioni
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1644 cm⁻¹ affidabilità 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 -
1640 cm⁻¹ affidabilità 1,0
“Text: 'peak located at 1640 which is indicative of a protein network primarily consisting of random coils'”
Gough 等 - 2020 - Air-Jet Spun Corn Zein Nanofibers and Thin Films w DOI: 10.3390/ijms21165780 -
3200 cm⁻¹ affidabilità 0,9
“Explicit assignment: 'band at 3200 ... relates to ν the peptide mode in the random coil structure'.”
Rozenberg 和 Shoham - 2007 - FTIR spectra of solid poly-L-lysine in the stretch DOI: 10.1016/j.bpc.2006.07.008 -
1655 cm⁻¹ affidabilità 0,9
“Second derivative spectrum component at ~1655 cm-1 assigned to α-helix and random coil structures.”
Ami 等 - 2022 - A Global Picture of Molecular Changes Associated t DOI: 10.3390/ijms232113447 -
1657 cm⁻¹ affidabilità 0,9
“Second derivative spectrum shows band at ~1657 cm-1 mainly due to alpha-helix and random-coil structures.”
Berterame 等 - 2016 - Protein aggregation and membrane lipid modificatio DOI: 10.1186/s12934-016-0438-2 -
1645 cm⁻¹ affidabilità 0,9
“Explicit assignment: 'position of the maximum of the amide I band of random coil ... 1645 cm-1'.”
Budyak 等 - 2008 - Flexibility of the cytoplasmic domain of the photo DOI: 10.1155/2008/267912 -
1645 cm⁻¹ affidabilità 0,9
“Loop to random coil transition at 1645 cm-1.”
Ye 等 - 2007 - Infrared spectroscopic discrimination between the DOI: 10.1529/biophysj.107.106799 -
1651 cm⁻¹ affidabilità 0,8
“Assigned to random coil and/or α-helix.”
Lin 等 - 2005 - PHand thermal-dependent conformational transitio DOI: 10.1016/j.peptides.2004.11.005
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