Infrared Probing of 4-Azidoproline Conformations Modulated by Azido Configurations
- Authors
- Lee, Kyung-Koo; Park, Kwang-Hee; Joo, Cheonik; Kwon, Hyeok-Jun; Jeon, Jonggu; Jung, Hyeon-Il; Park, Sungnam; Han, Hogyu; Cho, Minhaeng
- Issue Date
- 3-5월-2012
- Publisher
- AMER CHEMICAL SOC
- Citation
- JOURNAL OF PHYSICAL CHEMISTRY B, v.116, no.17, pp.5097 - 5110
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF PHYSICAL CHEMISTRY B
- Volume
- 116
- Number
- 17
- Start Page
- 5097
- End Page
- 5110
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/108456
- DOI
- 10.1021/jp1085119
- ISSN
- 1520-6106
- Abstract
- 4-Azidoproline (Azp) can tune the stability of the polyproline II (P-II) conformation in collagen. The azido group in the 4R and 4S configurations stabilizes and destabilizes the P-II conformation, respectively. To obtain insights into the dependence of the conformational stability on the azido configuration, we carried out Fourier transform (FT) IR experiments with four 4-azidoproline derivatives, Ac-(4R/S)-Azp-(NH/O)Me. We found that the amide I and azido IR spectra are different depending on the azido configuration and C-terminal structure. The origin of such spectral differences between 4R and 45 configurations and between C-terminal methylamide and ester ends was elucidated by quantum chemistry calculations in combination with H-1 NMR and time- and frequency-resolved IR pump-probe spectroscopy. We found that the azido configurations and C-terminal structures affect intramolecular interactions, which are responsible for the ensuing conformational and thereby IR spectral differences. Consequently, 4-azidoproline conformations modulated by azido configurations can be probed by IR spectroscopy. These findings suggest that 4-azidoproline can be both a structure-control and -probing element, which enables the infrared tracking of proline roles in protein structure, function, and dynamics.
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Collections - College of Science > Department of Chemistry > 1. Journal Articles
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