Date of Award
Fall 11-26-2013
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Physics
First Advisor
Eric Landahl, Ph.D.
Second Advisor
Anuj Sarma, Ph.D.
Third Advisor
Jesus Pando, Ph.D.
Abstract
The structural dynamics of the fusion protein (F protein) of parainfluenza virus 5 (PIV 5) was studied using time resolved Small Angle X-ray Scattering (SAXS). Conformational changes of the F protein, equivalent to the conformational changes the protein must undergo while infecting a host cell, are triggered by temperature jump to the protein in solution. The time and temperature dependence of the rate of the protein changing state is then determined through standard SAXS analysis. Thermodynamic transition state theory is then used to calculate the activation energy, enthalpy and entropy of the transition which is independent of any particular model. It is determined that the transition is entropically driven. Additionally a new technique employing constrained singular value decomposition is used to decompose the SAXS scattering patterns into basis states. The new technique successfully corroborates results found using the standard SAXS analysis.
Recommended Citation
Andorf, Matthew, "Time Resloved SAXS Analysis of Fusion Protein" (2013). College of Science and Health Theses and Dissertations. 63.
https://via.library.depaul.edu/csh_etd/63