Next Article in Journal
Genetic and Epigenetic Traits as Biomarkers in Colorectal Cancer
Next Article in Special Issue
Probing Kinetic Mechanisms of Protein Function and Folding with Time-Resolved Natural and Magnetic Chiroptical Spectroscopies
Previous Article in Journal
Identification of (−)(E)-N-[2(S)-Hydroxy-2-(4-hydroxyphenyl) ethyl]ferulamide, a Natural Product Isolated from Croton Pullei: Theoretical and Experimental Analysis
Previous Article in Special Issue
X-Ray Detected Magnetic Resonance: A Unique Probe of the Precession Dynamics of Orbital Magnetization Components
Article Menu

Export Article

Open AccessReview
Int. J. Mol. Sci. 2011, 12(12), 9404-9425; doi:10.3390/ijms12129404

Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy

Department of Chemistry, Yale University, 225 Prospect Street, New Haven, CT, 06520, USA
*
Author to whom correspondence should be addressed.
Received: 8 November 2011 / Revised: 13 December 2011 / Accepted: 13 December 2011 / Published: 16 December 2011
(This article belongs to the Special Issue Applications of Circular Dichroism)
View Full-Text   |   Download PDF [963 KB, uploaded 19 June 2014]   |  

Abstract

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.
Keywords: chirality; chiral sum frequency generation spectroscopy; amide I; N-H stretch; protein secondary structures; chiral vibrational structures of proteins; interfaces chirality; chiral sum frequency generation spectroscopy; amide I; N-H stretch; protein secondary structures; chiral vibrational structures of proteins; interfaces
Figures

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Fu, L.; Wang, Z.; Yan, E.C. Chiral Vibrational Structures of Proteins at Interfaces Probed by Sum Frequency Generation Spectroscopy. Int. J. Mol. Sci. 2011, 12, 9404-9425.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top