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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
Introduction and technical survey: protein aggregation and fibrillogenesis
J Robin Harris1, Nathaniel G N Milton
1Institute of Zoology, University of Mainz, 55099, Mainz, Germany, rharris@uni-mainz.de.
Sub-Cellular Biochemistry
|December 11, 2012
Summary
This chapter introduces protein aggregation and fibrillogenesis in amyloidogenesis, covering key topics and techniques. It provides a comprehensive overview of methods for studying protein oligomerization and aggregation.
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- Protein aggregation and fibrillogenesis are central to amyloidogenesis.
- Understanding these processes is crucial for both basic and clinical science.
- Numerous proteins and peptides are known to undergo fibrillogenesis.
Purpose of the Study:
- To provide a comprehensive background on protein aggregation and fibrillogenesis.
- To introduce the scope of topics covered in subsequent chapters.
- To survey the diverse techniques used to study these phenomena.
Main Methods:
- Tabulation of proteins and peptides involved in fibrillogenesis.
- Categorization of techniques into microscopical, analytical/biophysical, and biochemical/cellular methods.
- Literature references for detailed technique discussions.
Main Results:
- A structured overview of protein aggregation and fibrillogenesis.
- A classification of available research techniques.
- Identification of key proteins and peptides implicated in these processes.
Conclusions:
- The chapter establishes a foundational understanding of protein aggregation.
- It highlights the breadth of methodologies available for research.
- It serves as a guide to further exploration of amyloidogenesis.
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