| Biography | |
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 Prof. Guangnan Ou Jimei University, P. R. China, China |
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| Title: Ionization basis for activation of enzymes | |
| Abstract:
Proteins consist of both polar and nonpolar amino acids. In aqueous solution, globular proteins usually turn their polar groups outward, toward the aqueous solvent remaining hydrated, and their nonpolar groups inward, away from the water molecules leading to the hydrophobic effect that drives the folding of proteins into compact globular tertiary structures. The structures and behavior of enzymes is strongly dependent on the protonation state of their ionizable groups[1, 2]. The ionization shift may inactivate enzymes due to the alteration of protonation state of either ionizable groups directly involved in catalysis or those residues elsewhere that play a key role in the overall retention of the active enzyme conformation.
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| Biography:
Male, born on 22 Feb 1965, obtained his B.S. in chemistry at Sun Yat-sen University, China, in 1985, and his Ph.D. in physical chemistry at Xiamen University, China, in 2007. In 1991, he joined the faculty of Jimei University, China, where he is now associate professor of chemistry. He worked as an Academic Visitor under the supervision of Prof. Peter Halling at the University of Strathclyde for the period 1 September 2013 to 31 August 2014. His research interests focus on nonaqueous enzymatic catalysis, ionic liquid, chemical protein modification, and artificial enzyme. Recently, he proposed basic principles for biosolvent design on the viewpoint of ionization.
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