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Effect of isotope substitution on the Fermi resonance and vibrational lifetime of unnatural amino acids modified with IR probe: A 2D-IR and pump-probe study of 4-azido-L-phenyl alanine

Authors
Park, Jun YoungMondal, SaptarsiKwon, Hyeok-JunSahu, Prabhat KumarHan, HogyuKwak, KyungwonCho, Minhaeng
Issue Date
28-Oct-2020
Publisher
AMER INST PHYSICS
Citation
JOURNAL OF CHEMICAL PHYSICS, v.153, no.16
Indexed
SCIE
SCOPUS
Journal Title
JOURNAL OF CHEMICAL PHYSICS
Volume
153
Number
16
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/52094
DOI
10.1063/5.0025289
ISSN
0021-9606
1089-7690
Abstract
The infrared (IR) probe often suffers from an unexpected complex absorption profile due to the Fermi resonance and short vibrational lifetime, which restricts the application of time-resolved IR spectroscopy to investigate the site-specific structural dynamics of the protein. Researchers have found that isotope substitution to the IR probe not only removes the Fermi resonance but also extends the dynamic observation window with a prolonged vibrational lifetime. This method has been successfully applied to modify the vibrational properties of many IR probes for time-resolved spectroscopy and imaging. In this study, the effect of isotope substitution (N-15) on the vibrational properties of the azide stretching band in 4-azido-L-phenylalanine has been investigated using ultrafast pump-probe and 2D-IR spectroscopy. In contrast to the earlier reports, it has been observed that the Fermi resonance remains unchanged even after isotope substitution, and there is very little change in the vibrational relaxation dynamics as well. Anharmonic frequency analysis reveals that the alpha -N atom of N-3 is being shared between the two transitions participating in the Fermi resonance and gets affected similarly due to isotope labeling. Hence, this study unveils the specific circumstance at which the isotope labeling strategy may not be successful in eliminating the Fermi resonance band and explains the molecular origin behind it. This study also suggests definitive approaches on how to overcome the limitations related to the Fermi resonance to extend the development and application of this IR probe for biological research.
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