dc.contributor.advisor | Wilson, David P., 1976- | |
dc.contributor.author | Turton, Matt N. | |
dc.date.accessioned | 2020-06-13T12:57:53Z | |
dc.date.available | 2020-06-13T12:57:53Z | |
dc.date.issued | 2019-07-01 | |
dc.identifier.uri | https://cache.kzoo.edu/handle/10920/38583 | |
dc.description | 26 p. | en_US |
dc.description.abstract | Triangulation number is crucial for understanding the size of viral capsids and total number of proteins, but lacks in its ability to describe the conformational changes that occur throughout the maturation phase of spherical viruses. Maturation is a series of conformational changes that induce changes in the radial components of the viral proteins. Point arrays are further able to classify the maturation pathway of spherical viruses by showing at least one point per protein and allowing for the slight changes in conformation to be noted thoroughly. Point arrays also show the regions of the viral capsid that are unable to be altered, or else the structure of the viral capsid might be compromised. It can be seen from the results that when comparing viruses in native and mature forms, the best fitting point arrays changed. Out of the 11 viruses that had both native and mature forms, 9 viruses experienced changes in their best fitting point arrays. When comparing amino acids among gauge points, no correlations were found except glutamine and asparagine being the most common amino acids touching gauge points. | en_US |
dc.format.mimetype | application/pdf | |
dc.language.iso | en_US | en_US |
dc.relation.ispartof | Kalamazoo College Physics Senior Individualized Projects Collection | |
dc.rights | U.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder. All rights reserved. | |
dc.title | Utilizing Point Arrays to Further Classify Spherical Viruses Exhibiting Icosahedral Symmetry | en_US |
dc.type | Thesis | en_US |