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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...

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Detalles Bibliográficos
Autores principales: Fu, Li, Wang, Zhuguang, Yan, Elsa C.Y.
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
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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.
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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
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