Share Email Print

Proceedings Paper

Model calculations on the amide-I infrared bands of globular proteins
Author(s): Hajime Torii
Format Member Price Non-Member Price
PDF $17.00 $21.00

Paper Abstract

Model calculations are performed on the amide-I infrared (IR) bands of globular proteins. Coupling between peptide groups is introduced by the transition dipole coupling (TDC) mechanism. Good agreement is obtained between the calculated and observed amide-I band envelopes. In order to obtain detailed information on the structure-spectrum correlation, 3-D doorway-state theory is worked out and is applied to the spectra thus calculated. The E1- mode like motions of (alpha) -helices are shown to have large contributions to the IR intensity in the 1640 - 1630 cm-1 region of myoglobin, settling the question as to the origin of such bands observed for highly helical proteins. The differences in the amide-I band envelopes between (alpha) -lactalbumin and lysozyme are most probably due to the structural differences between the (alpha) -helical parts near the N-termini of these proteins.

Paper Details

Date Published: 31 January 1994
PDF: 2 pages
Proc. SPIE 2089, 9th International Conference on Fourier Transform Spectroscopy, (31 January 1994); doi: 10.1117/12.166718
Show Author Affiliations
Hajime Torii, Univ. of Tokyo (Japan)

Published in SPIE Proceedings Vol. 2089:
9th International Conference on Fourier Transform Spectroscopy
John E. Bertie; Hal Wieser, Editor(s)

© SPIE. Terms of Use
Back to Top