Scanning x-ray microdiffraction studies of the molecular architecture of biological tissues

Permanent URL: http://hdl.handle.net/2047/D20195172
Title:
Scanning x-ray microdiffraction studies of the molecular architecture of biological tissues
Creator:
Liu, Jiliang (Author)
Contributor:
Makowski, Lee (Advisor)
Kirschner, Daniel (Committee member)
Niedre, Mark (Committee member)
Language:
English
Publisher:
Boston, Massachusetts : Northeastern University, 2015
Date Accepted:
August 2015
Date Awarded:
August 2015
Type of resource:
Text
Genre:
Dissertations
Format:
electronic
Digital origin:
born digital
Abstract/Description:
X-ray scattering is an important method to study atomic and molecular structures. Here, I apply scanning x-ray micro-diffraction, a new advanced synchrotron technology, to study the molecular structure of three tissues: 1. Myelin within the peripheral nervous system (PNS); 2. Plant cell walls in Arabidopsis stems; 3. Protein aggregation in human brain sections from Alzheimer's patients. A suite of custom software was developed to overcome the challenge of processing a large amount of data collected by scanning micro diffraction and to extract complex features from the scattering patterns of these different tissues. These improvements in software have greatly expanded the utility scanning microdiffraction technology for analysis of detailed information about the molecular architecture of myelin in the nodal, paranodal, and juxtaparanodal regions; the structural heterogeneities within the Arabidopsis stem; and pathological molecular structures that arise in Alzheimer's disease. We anticipate significant expansion of the use of this method for studies of the molecular architecture of intact tissues and the alteration of these structures due to wounds, specific mutations or pathological conditions.
Subjects and keywords:
amyloid fibril
feature extraction
molecular stucture
scanning microdiffraction
X-rays -- Diffraction
X-rays -- Scattering
Arabidopsis -- Molecular aspects
Cellulose -- Structure
Myelin sheath -- Structure
Amyloid beta-protein -- Structure
Alzheimer's disease -- Molecular aspects
DOI:
https://doi.org/10.17760/D20195172
Permanent Link:
http://hdl.handle.net/2047/D20195172
Use and reproduction:
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