Theses and Dissertations
Studying Mechanical and Structural Properties of β-LG and β-CN Fibrils Using Atomic Force Microscopy
Date of Award
12-2018
Document Type
Thesis
Degree Name
Master of Science (MS)
Department
Physics
First Advisor
Dr. Ahmed Touhami
Second Advisor
Dr. Karen Martirosyan
Third Advisor
Dr. Andreas Hanke
Abstract
Amyloid fibrils from milk proteins have recently been the subject of extensive investigations in biophysics. The purpose of this thesis is to investigate the dynamics of fibrillation and the mechanical properties of β-LG and β-CN fibers using AFM-Quantitative Nanomechanical Mapping (QNM) and AFM-force spectroscopy. β-LG required one day of heating at 80 °C , pH 2 to fibrillate in solution; β-CN required three days. Using the AFM-QNM mode an average elastic modulus of 4.3 GPa was determined for the β-LG fibers and 3.1 GPa for β-casein fibers. A persistence length of 920 nm was determined using end to end distance and contour length data of β-LG fibers; for β-casein, a persistence length of 2200 nm was determined.
Recommended Citation
Villar, Hugo A., "Studying Mechanical and Structural Properties of β-LG and β-CN Fibrils Using Atomic Force Microscopy" (2018). Theses and Dissertations. 542.
https://scholarworks.utrgv.edu/etd/542
Comments
Copyright 2018 Hugo A. Villar. All Rights Reserved.
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