Ultrafast Solvation Dynamics of Subtilisin-Polyethylene Glycol Interaction for Protein Crystallization
DING Qing1, MENG Geng2, WANG Shu-Feng1**, ZHENG Xiao-Feng2, YANG Hong1, GONG Qi-Huang1
1State Key Laboratory for Mesoscopic Physics, Department of Physics, Peking University, Beijing 100871 2School of Life Sciences, Peking University, Beijing 100871
Ultrafast Solvation Dynamics of Subtilisin-Polyethylene Glycol Interaction for Protein Crystallization
DING Qing1, MENG Geng2, WANG Shu-Feng1**, ZHENG Xiao-Feng2, YANG Hong1, GONG Qi-Huang1
1State Key Laboratory for Mesoscopic Physics, Department of Physics, Peking University, Beijing 100871 2School of Life Sciences, Peking University, Beijing 100871
摘要We study the ultrafast solvation dynamics of protein-precipitant complexes. Protein subtilisin carlsberg (SC) was mixed with several polyethylene glycol (PEG) precipitants for protein crystallization. Picosecond-resolved emission spectra from single intrinsic tryptophan residue (Trp-113) are recorded to construct solvation correlation functions. For precipitant concentrations with various crystallization effects, we observe drastically different solvation relaxation processes. These differences in solvation dynamics are correlated with the local protein structural integrity and water-network stability upon interaction with the precipitants. The solvation dynamics at the protein surface is proposed as a new perspective to study precipitant-protein interactions.
Abstract：We study the ultrafast solvation dynamics of protein-precipitant complexes. Protein subtilisin carlsberg (SC) was mixed with several polyethylene glycol (PEG) precipitants for protein crystallization. Picosecond-resolved emission spectra from single intrinsic tryptophan residue (Trp-113) are recorded to construct solvation correlation functions. For precipitant concentrations with various crystallization effects, we observe drastically different solvation relaxation processes. These differences in solvation dynamics are correlated with the local protein structural integrity and water-network stability upon interaction with the precipitants. The solvation dynamics at the protein surface is proposed as a new perspective to study precipitant-protein interactions.
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2011, Vol. 28 
