Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 112, Issue 43, Pages 13473-13475Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp8061288
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Funding
- JSPS [19205005]
- MEXT [19056009]
- Grants-in-Aid for Scientific Research [19205005] Funding Source: KAKEN
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In situ characterization of Surface denaturation of a protein was realized by newly developed interface-selective multiplex electronic sum frequency generation spectroscopy. The observed electronic spectra of cytochrome c at the air/water interface exhibited a broad feature, which demonstrated coexistence of the nativelike and denatured protein at the interface. This situation of the mixed conformation at the air/water interface did not change in the acidic condition of pH = 2 where the protein was completely denatured in the bulk water. In sharp contrast, only native spectrum was observed at the silica/water interface.
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