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제117회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Protein and Chromophore Structural Dynamics in Signaling of Photoactive Yellow Protein Tracked by Time-resolved X-ray Solution Scattering and Optical Spectroscopy

2016년 2월 18일 14시 10분 49초
PHYS.O-5 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 09시 : 50분
물리화학 - 일반 구두발표 (General Oral Presentation)
저자 및
김태우, 김정호1, 이효철*
한국과학기술원(KAIST) 화학과, Korea
1인하대학교 화학과, Korea
Protein structural transition occurs via a sequence of protein conformational changes, which is systematically regulated by the perturbation of local structure such as a light-absorbing chromophore. It is a central theme of biophysics to understand how the global conformational change of a photoreceptor protein is temporally and spatially related with the local structural change around the light-absorbing chromophore. Among various photoreceptor proteins, we selected a mutant of photoactive yellow protein (PYP), which is responsible for signal reception of the negative phototaxis of the bacterium Halorhodospira halophila. Upon absorbing blue light, PYP undergoes a unique photocycle that leads to the expression of a signaling state accompanied by the global conformational change of the protein. In the mutant, the internal proton transfer from a Glu46 residue to the p-coumaric acid chromophore, which is a key step leading to the expression of signaling state, is prohibited due to the absence of internal proton donor. In this work, we used the combined probes of time-resolved X-ray solution scattering and optical spectroscopy. From the comparison of kinetic components identified by the combined probes, we found that the global conformational change involved in the transition to the signaling state is temporally delayed from the local structural change around the chromophore. In addition, from the time-resolved X-ray scattering signal containing the rich information on the protein conformation, we reveal that E46Q-PYP undergoes a transition to the putative signaling state accompanying smaller conformational changes than wild-type PYP.