James C. Patterson

Assistant Professor, Biophysical/Computational/Inorganic Chemistry


CHEM 256

B.A. in chemistry from Carleton College (1997)
Ph.D. in chemistry from the University of California
Santa Barbara (2004) - doctoral advisor Peter C. Ford
Postdoctoral fellow at UAB (2004-2007) studying apolipoproteins with Jere P. Segrest

Recent Publications:

Pan, L; Patterson, JC. Molecular dynamics study of Zn(Aβ) and Zn(Aβ)2. PLoS One., 2013, 8, e70681.

Research Interests

My research uses computational methods to study the reaction mechanisms of metalloenzymes and the dynamics of membrane-associated proteins. The main goal of my research is to elucidate the underlying chemical and biophysical causes of age- and stress-related diseases.

Computational Inorganic Chemistry

Cupins are a class of proteins that are found in every kingdom of life and have a wide range of functions. Cysteine dioxygenase (CDO) belongs to this superfamily of proteins, and it catalyzes the conversion of cysteine to cysteine sulfinic acid. This is the first step in cysteine catabolism, which has implications for neurodegenerative disorders like Alzheimer's, Parkinson's diseases and ALS.

Crystal structures for mouse, rat and human CDO are known. Although there are small structural differences in each, there are significant differences in the three proposed reaction mechanisms for how they function. These mechanisms were based on crystallographic and chemical intuition. My research uses density functional calculations to study these reaction mechanisms with the goal of identifying which reactive intermediates are energetically accessible, and which reaction pathways are most favorable. HumanCDO
Computational Biophysics

Alpha synuclein is a soluble presynaptic protein that has been found in the abnormal protein depositions of Lewy bodies and senile plaques of Parkinson’s and Alzheimer’s diseases, respectively. The aggregation (or oligomerization) of this protein are believed to play a critical role in the pathology of Parkinson's disease, but the mechanism by which this occurs is not well understood. 

Several researchers have suggested that transition metals play an important role in the pathogenesis of idiopathic Parkinson's disease.  While much critical experimental research continues in this area, very few computational studies have attempted to study á-synuclein dynamics.  My research combines molecular dynamics simulations and density functional theory calculations to study the dynamics of á-synuclein oligomerization, particularly in the presence of transition metals.