Unique Hydrogen Bonds in Membrane Protein Monitored by Whole Mid-IR ATR Spectroscopy in Aqueous Solution
| Autor: | Keiichi Inoue, Shota Ito, Hideki Kandori, Masayo Iwaki, Shinya Sugita, Rei Abe-Yoshizumi, Tatsuya Iwata |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Rhodopsin Infrared 010402 general chemistry 01 natural sciences 03 medical and health sciences Bacterial Proteins Spectroscopy Fourier Transform Infrared Materials Chemistry Physical and Theoretical Chemistry Fourier transform infrared spectroscopy Spectroscopy Binding Sites Aqueous solution biology Hydrogen bond Chemistry Sodium Water Hydrogen Bonding 0104 chemical sciences Surfaces Coatings and Films Crystallography 030104 developmental biology Membrane protein Attenuated total reflection biology.protein Flavobacteriaceae |
| Zdroj: | The Journal of Physical Chemistry B. 122:165-170 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.7b11064 |
| Popis: | Protein function is coupled to its structural changes, for which stimulus-induced difference Fourier-transform infrared (FTIR) spectroscopy is a powerful method. By optimizing the attenuated total reflection (ATR)-FTIR analysis on sodium-pumping rhodopsin KR2 in aqueous solution, we first measured the accurate difference spectra upon sodium binding in the whole IR region (4000-1000 cm-1). The new spectral window allows the analysis of not only the fingerprint region (1800-1000 cm-1) but also the hydrogen-bonding donor region (4000-1800 cm-1), revealing an unusually strong hydrogen bond of Tyr located in the sodium binding site of KR2. Progress in ATR-FTIR difference spectroscopy provides an approach to investigating stimulus-induced structural changes of membrane proteins under physiological aqueous conditions. |
| Databáze: | OpenAIRE |
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