Document Type



Doctor of Philosophy



First Adviser

Gunton, James D.


There are many things in the world that are not spheres. As a result, isotropic interaction potentials can only serve as a crude approximation to complex molecules such as proteins. In order to better understand the often harmful self-assembly phenomena that proteins can undergo, study of how anisotropic features alter collective behavior is required. Beyond the biological, these lessons can also guide rational design of new materials in the area of colloidal science. This dissertation examines the role of specific anisotropic features in coarse-grained representations of three proteins that undergo self-assembly processes. The first, amelogenin, is the primary protein involved in the formation of dental enamel; chapter 2 will explore the effect of the charged hydrophilic tail on the phase diagram of this otherwise hydrophobic protein. In chapter 3, the role of hinge angle between binding sites will be assessed in a simplified model of human antibodies; this angle has dramatic effect on aggregate morphology. Lastly, in chapter 4, the nucleation and growth mechanisms of polyglutamine tracts of different lengths will be studied, relevant to the formation of a class of neurodegenerative diseases, including Huntington's Disease. This process shows a strong dependence on repeat length, and at shorter lengths, variation due to concentration.