Cargando…
Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy
We review the recent development of chiral sum frequency generation (SFG) spectroscopy and its applications to study chiral vibrational structures at interfaces. This review summarizes observations of chiral SFG signals from various molecular systems and describes the molecular origins of chiral SFG...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257137/ https://www.ncbi.nlm.nih.gov/pubmed/22272140 http://dx.doi.org/10.3390/ijms12129404 |
_version_ | 1782221111836016640 |
---|---|
author | Fu, Li Wang, Zhuguang Yan, Elsa C.Y. |
author_facet | Fu, Li Wang, Zhuguang Yan, Elsa C.Y. |
author_sort | Fu, Li |
collection | PubMed |
description | We review the recent development of chiral sum frequency generation (SFG) spectroscopy and its applications to study chiral vibrational structures at interfaces. This review summarizes observations of chiral SFG signals from various molecular systems and describes the molecular origins of chiral SFG response. It focuses on the chiral vibrational structures of proteins and presents the chiral SFG spectra of proteins at interfaces in the C-H stretch, amide I, and N-H stretch regions. In particular, a combination of chiral amide I and N-H stretches of the peptide backbone provides highly characteristic vibrational signatures, unique to various secondary structures, which demonstrate the capacity of chiral SFG spectroscopy to distinguish protein secondary structures at interfaces. On the basis of these recent developments, we further discuss the advantages of chiral SFG spectroscopy and its potential application in various fields of science and technology. We conclude that chiral SFG spectroscopy can be a new approach to probe chiral vibrational structures of protein at interfaces, providing structural and dynamic information to study in situ and in real time protein structures and dynamics at interfaces. |
format | Online Article Text |
id | pubmed-3257137 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-32571372012-01-23 Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy Fu, Li Wang, Zhuguang Yan, Elsa C.Y. Int J Mol Sci Review We review the recent development of chiral sum frequency generation (SFG) spectroscopy and its applications to study chiral vibrational structures at interfaces. This review summarizes observations of chiral SFG signals from various molecular systems and describes the molecular origins of chiral SFG response. It focuses on the chiral vibrational structures of proteins and presents the chiral SFG spectra of proteins at interfaces in the C-H stretch, amide I, and N-H stretch regions. In particular, a combination of chiral amide I and N-H stretches of the peptide backbone provides highly characteristic vibrational signatures, unique to various secondary structures, which demonstrate the capacity of chiral SFG spectroscopy to distinguish protein secondary structures at interfaces. On the basis of these recent developments, we further discuss the advantages of chiral SFG spectroscopy and its potential application in various fields of science and technology. We conclude that chiral SFG spectroscopy can be a new approach to probe chiral vibrational structures of protein at interfaces, providing structural and dynamic information to study in situ and in real time protein structures and dynamics at interfaces. Molecular Diversity Preservation International (MDPI) 2011-12-16 /pmc/articles/PMC3257137/ /pubmed/22272140 http://dx.doi.org/10.3390/ijms12129404 Text en © 2011 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Fu, Li Wang, Zhuguang Yan, Elsa C.Y. Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy |
title | Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy |
title_full | Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy |
title_fullStr | Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy |
title_full_unstemmed | Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy |
title_short | Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy |
title_sort | chiral vibrational structures of proteins at interfaces probed by sum frequency generation spectroscopy |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257137/ https://www.ncbi.nlm.nih.gov/pubmed/22272140 http://dx.doi.org/10.3390/ijms12129404 |
work_keys_str_mv | AT fuli chiralvibrationalstructuresofproteinsatinterfacesprobedbysumfrequencygenerationspectroscopy AT wangzhuguang chiralvibrationalstructuresofproteinsatinterfacesprobedbysumfrequencygenerationspectroscopy AT yanelsacy chiralvibrationalstructuresofproteinsatinterfacesprobedbysumfrequencygenerationspectroscopy |