## Abstract In this work we employed UV resonance Raman spectroscopy with 229 nm excitation to study two tryptophan‐containing antimicrobial peptides with a broad‐spectrum activity against Gram‐positive and Gram‐negative bacteria: lactoferricin B (LfB, RRWQWRMKKLG) and pEM‐2 (KKWRWWLKALAKK). UV res
Visible and UV-resonance Raman spectroscopy of model peptides
✍ Scribed by Reinhard Schweitzer-Stenner
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 740 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0377-0486
- DOI
- 10.1002/jrs.757
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✦ Synopsis
Abstract
We review various visible and UV‐resonance Raman experiments on model peptides such as N‐methylacetamide and di‐ and triglycine which are aimed at exploring the structure and dynamics of these molecules. Whereas visible Raman spectroscopy probes the electronic ground state, the UV Raman technique is utilized additionally to obtain structural information about excited electronic states. This research is aimed at obtaining a spectroscopically determined force field, which can be transferred to polypeptides and proteins. We further argue that the capability of vibrational spectroscopy to probe the structure of peptides and proteins can be significantly improved by combining computational and spectroscopic studies on appropriate model peptides to calibrate wavenumbers and intensities of Raman and IR bands for the quantitative determination of structural parameters such as the dihedral angles. Copyright © 2001 John Wiley & Sons, Ltd.
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