Abstract
The curve-fitted Fourier-transform infrared spectrum of linear turn-forming peptides was found to contain an amide I component band near or below 1640 cm-1, similarly to the IR spectra of cyclic β-turn models. This band, termed β-turn band, is due to the CO stretching vibrational mode of the acceptor amide group involved in a strong 1←4 H-bond. H-bondings are chiral constraints because they stabilize helical or folded conformations with only one (right or left) sense of handedness. This makes the combination of CD and FT-IR spectroscopy a unique tool for characterizing the absolute conformation of polypeptides.
| Original language | English |
|---|---|
| Pages (from-to) | 591-603 |
| Number of pages | 13 |
| Journal | Tetrahedron Asymmetry |
| Volume | 4 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1993 |
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ASJC Scopus subject areas
- Inorganic Chemistry
- Organic Chemistry
- Materials Chemistry
- Drug Discovery
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FT-IR spectroscopy guided analysis of the circular dichroism spectra of polypeptides. / Perczel, András; Majer, Zsuzsa; Holly, Sándor; Machytka, Daisy; Fasman, Gerald D.; Hollósi, Miklós.
In: Tetrahedron Asymmetry, Vol. 4, No. 3, 1993, p. 591-603.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - FT-IR spectroscopy guided analysis of the circular dichroism spectra of polypeptides
AU - Perczel, András
AU - Majer, Zsuzsa
AU - Holly, Sándor
AU - Machytka, Daisy
AU - Fasman, Gerald D.
AU - Hollósi, Miklós
PY - 1993
Y1 - 1993
N2 - The curve-fitted Fourier-transform infrared spectrum of linear turn-forming peptides was found to contain an amide I component band near or below 1640 cm-1, similarly to the IR spectra of cyclic β-turn models. This band, termed β-turn band, is due to the CO stretching vibrational mode of the acceptor amide group involved in a strong 1←4 H-bond. H-bondings are chiral constraints because they stabilize helical or folded conformations with only one (right or left) sense of handedness. This makes the combination of CD and FT-IR spectroscopy a unique tool for characterizing the absolute conformation of polypeptides.
AB - The curve-fitted Fourier-transform infrared spectrum of linear turn-forming peptides was found to contain an amide I component band near or below 1640 cm-1, similarly to the IR spectra of cyclic β-turn models. This band, termed β-turn band, is due to the CO stretching vibrational mode of the acceptor amide group involved in a strong 1←4 H-bond. H-bondings are chiral constraints because they stabilize helical or folded conformations with only one (right or left) sense of handedness. This makes the combination of CD and FT-IR spectroscopy a unique tool for characterizing the absolute conformation of polypeptides.
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UR - http://www.scopus.com/inward/citedby.url?scp=0027483203&partnerID=8YFLogxK
U2 - 10.1016/S0957-4166(00)86099-1
DO - 10.1016/S0957-4166(00)86099-1
M3 - Article
AN - SCOPUS:0027483203
VL - 4
SP - 591
EP - 603
JO - Tetrahedron Asymmetry
JF - Tetrahedron Asymmetry
SN - 0957-4166
IS - 3
ER -