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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

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Title
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
Author(s)
Jun Young Park; Saptarsi Mondal; Kwon, H.-J.; Prabhat Kumar Sahu; Han, H.; Kyungwon Kwak; Minhaeng Cho
Subject
INFRARED PROBES, ; DYNAMICS, ; SPECTROSCOPY, ; PROTEINS, ; AZIDOHOMOALANINE, ; SENSITIVITY, ; RELAXATION, ; ISONITRILE, ; REPORTER, ; UTILITY
Publication Date
2020-10
Journal
JOURNAL OF CHEMICAL PHYSICS, v.153, no.16, pp.164309
Publisher
AMER INST PHYSICS
Abstract
© 2020 Author(s). 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 (15N) 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 α-N atom of N3 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
URI
https://pr.ibs.re.kr/handle/8788114/7581
DOI
10.1063/5.0025289
ISSN
0021-9606
Appears in Collections:
Center for Molecular Spectroscopy and Dynamics(분자 분광학 및 동력학 연구단) > 1. Journal Papers (저널논문)
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