Weihong Qiu, Luyuan Zhang, Oghaghare Okobiah, Yi Yang, Ultrafast Solvation Dynamics of Human Serum Albumin: Correlation with Conformational Transitions and Site-Selected Recognition Weihong Qiu, Luyuan Zhang, Oghaghare Okobiah, Yi Yang, Lijuan Wang, Ahmed H. Zewail and Dongping Zhong Biophysics Program The Ohio State University
Tryptophan: the Most Appropriate Fluorescence Probe in Proteins No concerns of spatial uncertainty Allow single-residue spatial resolution Easy incorporation in proteins with site- directed mutagenesis method
Conformational Transitions E F N B A Human Serum Albumin: Remarkable Drug Delivery Machinery & pH-Dependent Conformation Transition Conformational Transitions E F N B A pH Values 2.7 4.3 8 10.0
Solvation Dynamics: the Concept Pal, S.K.; Peon, J.; Bagchi, B. and Zewail, A.H. J.Phys. Chem. B 2002, 106, 12376
Femtosecond Up-Conversion Apparatus
Human Serum Albumin: Normal Form
Human Serum Albumin: Fast-Migrating Form
Human Serum Albumin: Extended Form
Conformation-Dependent Solvation Dynamics
Femtosecond-Resolved Rotational Anisotropy Tryptophan residue has the largest rotational freedom in N-form HSA
Conformational Transitions and Solvation Dynamics: the Correlation 108 ps 186 ps 133 ps 46 ps 27 ps
Conclusions We found the ligand-binding pocket is highly flexible. We established the correlation between the conformational transition of HSA and the observed solvation dynamics at the ligand-binding pocket.
Acknowledgements Dr. Dongping Zhong Dr. Ahmed H. Zewail Luyuan Zhang Oghaghare Okobiah Yi Yang Lijuan Wang Petroleum Research Foundation National Science Foundation