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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국광과학회 Rapid communication in photoscience : RCP Rapid communication in photoscience : RCP 제5권 제2호
- 발행연도
- 2016.1
- 수록면
- 18 - 20 (3page)
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초록· 키워드
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Through quantum chemical means, we inspect the energetics of the singlet oxygen formation with fluorescent proteins in their triplet excited states. By placing an oxygen molecule at varying distances, we discover that the energetic driving force for the singlet oxygen formation does not depend strongly on the chromophore $-O_2$ distance. We also observe that the chromophore vibrations contribute much to the energy gap modulation toward the surface crossing. Based on our computational results, we try to draw a series of rationalizations of different photostabilities of different fluorescent proteins. Most prominently, we argue that the chance of encountering a surface crossing point is higher with a protein with a lower photostability.
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