Senior Theses

Publication Date

5-18-2016

Document Type

Thesis (Linfield Access)

Degree Name

Bachelor of Science in Physics

Department

Physics

Faculty Advisor(s)

Joelle Murray (Thesis Advisor)
Michael Crosser & Keron Subero (Committee Members)

Subject Categories

Biological and Chemical Physics | Physics

Abstract

Proteins are known to fold into tertiary structures that determine their functionality in living organisms. However, the complex dynamics of protein folding and the way they consistently fold into the same structures is unknown. Experimental studies of the folding process are difficult as proteins are made of more than one subunit and possess a high degree of conformational flexibility. Theoretically, self-organized criticality (SOC) has provided a framework for understanding complex systems in various scientific disciplines through scale invariance and the associated "fractal" power law behavior. Evidence of this criticality phenomena has been found in neural systems, cell cultures, and anesthetized animals. In this research, we use a simple hydrophobic-polar lattice-bound computational model to investigate self-organized criticality as a possible mechanism for generating complexity in protein folding.

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