Format

Send to

Choose Destination
Chirality. 2014 Sep;26(9):521-4. doi: 10.1002/chir.22306. Epub 2014 Mar 7.

N-H stretching modes around 3300 wavenumber from peptide backbones observed by chiral sum frequency generation vibrational spectroscopy.

Author information

1
Departmtent of Chemistry, Yale University, New Haven, CT.

Abstract

We present a detailed analysis of the molecular origin of the chiral sum frequency generation (SFG) signals of proteins and peptides at interfaces in the N-H stretching vibrational region. The N-H stretching can be a probe for investigating structural and functional properties of proteins, but remains technically difficult to analyze due to the overlapping with the O-H stretching of water molecules. Chiral SFG spectroscopy offers unique tools to study the N-H stretching from proteins at interfaces without interference from the water background. However, the molecular origin of the N-H stretching signals of proteins is still unclear. This work provides a justification of the origin of chiral N-H signals by analyzing the vibrational frequencies, examining chiral SFG theory, studying proton (hydrogen/deuterium) exchange kinetics, and performing optical control experiments. The results demonstrate that the chiral N-H stretching signals at ~3300 cm(-1) originate from the amide group of the protein backbones. This chiral N-H stretching signal offers an in situ, real-time, and background-free probe for interrogating the protein structures and dynamics at interfaces at the molecular level.

KEYWORDS:

N-H stretching; protein backbones; vibrational mode

PMID:
24610602
DOI:
10.1002/chir.22306
[Indexed for MEDLINE]

Supplemental Content

Loading ...
Support Center