| Literature DB >> 15779931 |
Xiaoyun Chen1, Jie Wang, Jason J Sniadecki, Mark A Even, Zhan Chen.
Abstract
We demonstrated that sum frequency generation (SFG) vibrational spectroscopy can distinguish different secondary structures of proteins or peptides adsorbed at solid/liquid interfaces. The SFG spectrum for tachyplesin I at the polystyrene (PS)/solution interface has a fingerprint peak corresponding to the B1/B3 mode of the antiparallel beta-sheet. This peak disappeared upon the addition of dithiothreitol, which can disrupt the beta-sheet structure. The SFG spectrum indicative of the MSI594 alpha-helical structure was observed at the PS/MSI594 solution interface. This research validates SFG as a powerful technique for revealing detailed secondary structures of interfacial proteins and peptides.Entities:
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Year: 2005 PMID: 15779931 DOI: 10.1021/la050048w
Source DB: PubMed Journal: Langmuir ISSN: 0743-7463 Impact factor: 3.882