Journal of Undergraduate Research
Keywords
simulation, experiment, multi-state protein folding
College
Ira A. Fulton College of Engineering and Technology
Department
Chemical Engineering
Abstract
Proteins are made up of extremely long chains of amino acids. Depending on it constituent amino acids, proteins fold in many 3-dimensional patterns to facilitate various biochemical processes such as catalyzing chemical reactions which allow us to live. How proteins fold is thought to be the “holy grail” of biochemistry research and, as of yet, no one has been able to predict exactly how a given sequence of amino acids will fold a priori. Protein folding has been probed in experiment and simulated on computers, but there are discrepancies between the two methods. Naturally, the experimental results are what computer simulations aim to achieve as a test of their validity. Two major discrepancies between computer simulations and experiments are the narrowness of the protein folding transitions and the number of transitions seen in larger proteins.
Recommended Citation
Lewis, Jacob and Knotts, Dr. Thomas
(2013)
"Bridging the Gap Between Simulation and Experiment with Multi-State Protein Folding,"
Journal of Undergraduate Research: Vol. 2013:
Iss.
1, Article 1774.
Available at:
https://scholarsarchive.byu.edu/jur/vol2013/iss1/1774