ChemRxiv
These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
JPCL Cα-H Chirality Control N-H Chirality (20191119)-HFW20191124.pdf (1.19 MB)

N–H Chirality in Folded Peptide LK7β is Governed by the Cα–H Chirality

preprint
submitted on 24.11.2019, 08:03 and posted on 09.12.2019, 11:27 by Xiaohua Hu, Li Fu, jian hou, yuening zhang, Zhen Zhang, Hongfei Wang
Recent chiral sum-frequency generation vibrational spectroscopy (cSFG-VS) measurements revealed that the two N-H stretching modes in the 3000-3500 cm-1 range in folded protein and peptide exhibit chiral characteristics. Here we report the first phase-resolved sub-wavenumber high-resolution broadband SFG-VS (HR-BB-SFG-VS) measurement of the LK7β peptide. The results show that this chiral N-H band consists of four, instead of two, distinctive peaks, and they are with two groups of opposite spectral phases. Moreover, the phases of these N-H peaks completely flip from the L-LK7β to the D-LK7β peptide, suggesting that the chirality of the N-H in the folded LK7β peptide is completely governed by the chirality of the Cα–H of the amino acids. This discovery provides clue on why proteins in nature are composed of α-amino acids rather than β- or γ-amino acids, and may help us understand the question on the origin of life.

History

Email Address of Submitting Author

wanghongfei@fudan.edu.cn

Institution

Fudan University

Country

China

ORCID For Submitting Author

0000-0001-8238-1641

Declaration of Conflict of Interest

No

Exports

Read the published paper

in The Journal of Physical Chemistry Letters

ChemRxiv

Exports