Two-dimensional Fourier-transform infrared correlation spectroscopy study of the high-pressure tuning of proteins |
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| Affiliation: | 1. Department of Physiology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo, Japan;2. Department of Pharmaceutical Sciences, Faculty of Pharmacy, Keio University, 1-5-30 Shibakoen, Minato-ku, Tokyo, Japan;3. Department of Neurology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo, Japan;4. Department of Neurology and Stroke, Saitama Medical University International Medical Center, 1397-1 Yamane, Hidaka-shi, Saitama, Japan |
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| Abstract: | 2D FTIR gives new information about the pressure effect on the structure and dynamics of macromolecular systems. Application of this analysis to proteins can unravel the relation of conformational changes and H/D exchange processes. For lipoxygenase, a pressure of 6.5 kbar induces irreversible conformational changes resulting in an increased exposure of interior parts of the protein to the solvent. At the transition pressure the spectral changes indicate a correlation between conformational changes and H/D exchange. Below and above this pressure, the effects of H/D exchange on the spectral changes are predominant. |
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