(93ai) Mathematically Modeling the Kinetics of Protein Folding | AIChE

(93ai) Mathematically Modeling the Kinetics of Protein Folding

Authors 

Ackermann, K. L. - Presenter, Rowan University
Leighty, R. - Presenter, Rowan University


Diseases such as Alzhiemer's, Parkinson's and mad cow disease are caused by disfunctional proteins or aggregates. A potential cure for this problem may be found in the kinetics the protein's folding reactions. The reaction kinetics are believed to be a function of concentration and temperature, it may be possible to run the reaction under favorable conditions which would minimize the aggregation reaction and maximize the folding reaction. Thus far a kinetic model for P22 tailspike protein has been developed using Matlab® software. This reaction network consists of seven reactions; three folding reactions and five aggregation reactions. Experimental data for the concentration of each species were compared to a set of data generated by a series of differential equations. The error between the two sets was then minimized to determine the kinetic rate constants for each reaction. Rate constants have been determined for wild type P22 tailspike protein at 30 and 37 degrees Celsius, further modeling is planned for wild type P22 tailspike at other temperatures including 20 and 25 degrees Celcius and on mutant tailspike DN protein at various temperatures. Furthermore, the model developed can also be modified and applied to other proteins with different reaction networks.