FT-IR spectroscopy guided analysis of the circular dichroism spectra of polypeptides

András Perczel, Zsuzsa Majer, Sándor Holly, Daisy Machytka, Gerald D. Fasman, Miklós Hollósi

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 languageEnglish
Pages (from-to)591-603
Number of pages13
JournalTetrahedron Asymmetry
Volume4
Issue number3
DOIs
Publication statusPublished - 1993

Fingerprint

Polypeptides
polypeptides
Dichroism
Circular Dichroism
Amides
dichroism
Conformations
Infrared spectroscopy
Spectrum Analysis
Peptides
Functional Laterality
amides
Fourier Analysis
Carbon Monoxide
spectroscopy
Stretching
handedness
Fourier transforms
Infrared radiation
peptides

ASJC Scopus subject areas

  • Inorganic Chemistry
  • Organic Chemistry
  • Materials Chemistry
  • Drug Discovery

Cite this

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 journalArticle

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