Journal article
Secondary structure analysis of polypeptides by a model utilizing excitonic coupling between amide I modes
Polymeric materials science and engineering, Vol.91(fall)
01 Oct 2004
Abstract
The amide I band in the IR and to a less extent in the Raman spectra of polypeptides and proteins are frequently used to determine their secondary structure composition. The structural sensitivity of the corresponding amide I mode, which is predominantly a CO stretching vibration, is generally attributed to the influence of hydrogen bonding on the force constant of the carbonyl bond. Even though less emphasized, however, it is clear that vibrational mixing between amide I modes rather than hydrogen bonding provide the degree of structure sensitivity which distinguishes amide I from other backbone modes like amide II and III. In spite of numerous theoretical studies on amide I, no attempt has been undertaken thus far to obtain a more quantitative understanding of the relationship between amide I band profiles and peptide/protein structure. Recent attempts in this direction mostly dealt with very short model peptides for which bands assignable to individual amide I modes can still be identified. In this paper we extent these approaches to obtain a physical model which allows the simulation of the IR, Raman and Vibrational Circular Dichroism band profiles for intermediate sized peptides, which can be considered as representative of the length of structural motifs in proteins.
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Details
- Title
- Secondary structure analysis of polypeptides by a model utilizing excitonic coupling between amide I modes
- Creators
- Reinhard Schweitzer-Stenner
- Publication Details
- Polymeric materials science and engineering, Vol.91(fall)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Identifiers
- 991019170503704721