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Senior Lecturer in Computational Chemistry
Pharmaceutical, Chemical & Environmental Sciences
Dr Jiayun Pang joined the School of Science at the University of Greenwich in October, 2011.
Dr Pang received her BSc in Medicinal Chemistry from Shenyang Pharmaceutical University, China in 2001, and her PhD in Computational Chemistry from the University of Birmingham in 2006. She then moved to the University of Manchester to work as a postdoctoral research associate.
She is a recipient of the Royal Society of Chemistry Rita and John Cornforth Award in 2009.
Our knowledge of enzyme-catalysed reactions has traditionally been gained from crystallography and solution studies. However, due to rapid developments in computer power and software, computational tools are playing an increasingly important role in obtaining an atomistic understanding of how enzymes achieve enormous rate accelerations.
The computational approaches can reveal aspects of a reaction that are difficult to access through experiment. Thus, combining the strength of the two can provide very detailed insight into enzyme catalysis, the knowledge of which could lead to the development of new drugs (most function as inhibitors of enzymes) and the design of efficient catalysts with many industrial applications.
Dr Pang's research aims at elucidating, from the quantum phenomenon to the macromolecular levels, fundamental mechanisms of enzyme activity. The current focus is to explore how protein dynamics - ranging from local atomic vibrations on a femto to picosecond time scale to larger global domain motions that typically occur on a time scale of micro to millisecond - intrinsically correlate with the catalytic process.
A variety of computational approaches are employed, with emphasis on the application of the combined QM/MM methods and the development of new methodology and algorithms to achieve more realistic simulation of complex enzyme-catalysed reactions and broadly chemically/biologically relevant events.
Pang J, Li X, Morokuma K, Scrutton NS and Sutcliffe MJ (2012) Large-scale domain conformational change is coupled to the activation of the Co-C bond in the B12-dependent enzyme ornithine 4,5-aminomutase: a computational study. J. Am. Chem. Soc. 134, 2367-2377.
Pang J, Scrutton NS, de Visser SP and Sutcliffe MJ (2010) New insights into the multi-step reaction pathway of the reductive half-reaction catalysed by aromatic amine dehydrogenase: a QM/MM study. Chem. Commun. (Camb). 46, 3104-3106.
Pang J, Scrutton NS, de Visser SP and Sutcliffe MJ (2010). Assignment of the vibrational spectra of enzyme-bound tryptophan tryptophyl quinones using a combined QM/MM approach. J. Phys. Chem. A. 114, 1212-1217.
Hay S, Pudney CR, McGrory T, Pang J, Sutcliffe MJ and Scrutton NS (2009). Barrier compression enhances an enzymatic H-transfer reaction. Angew. Chem. Int. Ed. 48, 1452-1454.
Pang J, Hay S, Scrutton NS and Sutcliffe MJ (2008) Deep tunneling dominates the biologically important hydride transfer reaction from NADH to FMN in morphinone reductase. J. Am. Chem. Soc. 130, 7092-7097.
Pudney CR, Hay S, Pang J, Costello C, Leys D, Sutcliffe MJ and Scrutton NS (2007). Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies potential ambiguity in kinetic analysis of enzyme tunneling mechanisms. J. Am. Chem. Soc. 129, 13949-13956.
Pang J and Allemann RK (2007) Molecular dynamics simulation of thermal unfolding of Thermatoga maritima DHFR. Phys. Chem. Chem. Phys. 9, 711-718.
Pang J, Pu J, Gao J, Truhlar DG and Allemann RK (2006) Hydride transfer reaction catalyzed by hyperthermophilic dihydrofolate reductase is dominated by quantum mechanical tunneling and is promoted by both inter- and intramonomeric correlated motions. J. Am. Chem. Soc.128, 8015-8023.