2015
DOI: 10.1039/c5cc02263k
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The 13C amide I band is still sensitive to conformation change when the regular amide I band cannot be distinguished at the typical position in H2O

Abstract: The attenuated total reflection technique was utilized to obtain FTIR spectra of (13)C-labeled peptides with a sequence of (AAAAK)4AAAAY in H2O. The regular amide I band was not at the typical position as reported in globular proteins, whereas the (13)C amide I band was still sensitive to conformation change.

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Cited by 9 publications
(8 citation statements)
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“…3a,c , which was unique to the protein secondary structure. Such regions were designated as amides I and II, respectively 30 . In Fig.…”
Section: Resultsmentioning
confidence: 99%
“…3a,c , which was unique to the protein secondary structure. Such regions were designated as amides I and II, respectively 30 . In Fig.…”
Section: Resultsmentioning
confidence: 99%
“…[15] Two regions(1700 cm À 1 to 1600 cm À 1 and 1560 cm À 1 to 1500 cm À 1 ) were unique to the protein secondary structure, which could be designated as amides I and II, respectively. [16] Here the typical absorption peaks of protein-organic nanoflowers occurred at 1633 cm À 1 and 1554 cm À 1 for CONH and 2800-3600 cm À 1 for CH 2 and CH 3 . [17] Meanwhile, compared with the spectrum of Cu 3 (PO 4 ) 2 @BSA, the spectrum of Cu 3 (PO 4 ) 2 @BSA@Ag 3 PO 4 hybrid nanoflowers showed similar adsorption peaks, indicating that Ag 3 PO 4 was immobilized via self-assembly.…”
Section: Chemistryselectmentioning
confidence: 79%
“…While the peaks at 608 and 565 cm −1 could be attributed to the ν4 bending mode of the O=P−O bond, which contributes to the phosphate groups [15] . Two regions(1700 cm −1 to 1600 cm −1 and 1560 cm −1 to 1500 cm −1 ) were unique to the protein secondary structure, which could be designated as amides I and II, respectively [16] . Here the typical absorption peaks of protein‐organic nanoflowers occurred at 1633 cm −1 and 1554 cm −1 for CONH and 2800–3600 cm −1 for CH 2 and CH 3 [17] .…”
Section: Resultsmentioning
confidence: 97%
“…A shift in the band regions of 1650–1545 cm −1 and a band at 1601 cm −1 , which characterize the sensitive EV population, enabled to unambiguously distinguish spectra of EVs/s and EVs/DXR. This could be ascribed to a modification of the Amide I band and of the α-helix conformation [ 54 ]. Indeed, in FTIR spectroscopy, different peak positions of the Amide I band in the 1600 to 1700 cm −1 area correlate to different secondary structures of the proteins (i.e., unstructured conformation vs. α-helix conformation) and can be used to monitor conformation changes in proteins/peptides [ 55 , 56 ].…”
Section: Discussionmentioning
confidence: 99%