title: Chiral vibrational structures of proteins at interfaces probed by sum frequency generation spectroscopy.
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.
authors.affiliation: Department of Chemistry, Yale University, 225 Prospect Street, New Haven, CT, 06520, USA. li.fu@yale.edu
authors.forename: Li
authors.initials: L
authors.lastname: Fu
authors.forename: Zhuguang
authors.initials: Z
authors.lastname: Wang
authors.forename: Elsa C Y
authors.initials: EC
authors.lastname: Yan
mesh_terms: D000595:Amino Acid Sequence; D007536:Isomerism; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods*; D014732:Vibration
chemical_list: D011506:Proteins