Date on Master's Thesis/Doctoral Dissertation
4-2018
Document Type
Master's Thesis
Degree Name
M. Eng.
Department
Chemical Engineering
Committee Chair
Jaeger, Vance W.
Committee Co-Chair (if applicable)
Starr, Thomas
Committee Member
Starr, Thomas
Committee Member
Rouchka, Eric
Author's Keywords
Molecular dynamics; Proteins; Sum Frequency Generation; SFG
Abstract
Sum frequency generation (SFG) spectroscopy is an experimental technique for differentiating between various conformations and orientations of interfacial proteins. Combining a theoretical framework for SFG with molecular dynamics (MD) simulations provides a powerful tool for studying systems containing interfacial proteins with applications in cell transport, biofilms, and fermentation processes. Roeters’ method was used to calculate theoretical SFG responses for a variety of individual α-helix and β-sheet peptide secondary structures simulated using MD. Results show how the shape and locations of SFG amide I responses change with differences in hydrogen bonding patterns, peptide orientations, and SFG polarization combinations. The data presented herein demonstrate the utility of SFG spectroscopy for uniquely describing the orientation and conformation of interfacial proteins and how molecular simulation and theoretical spectral calculations complement this experimental technique.
Recommended Citation
Adams, Andrew J., "Sum frequency generation spectroscopy of simulated protein secondary structures." (2018). Electronic Theses and Dissertations. Paper 2893.
https://doi.org/10.18297/etd/2893
