| Chapter title |
Deep UV Resonance Raman Spectroscopy for Characterizing Amyloid Aggregation
|
|---|---|
| Chapter number | 6 |
| Book title |
Protein Amyloid Aggregation
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-2978-8_6 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-2977-1, 978-1-4939-2978-8
|
| Authors |
Joseph D. Handen, Igor K. Lednev |
| Abstract |
Deep UV resonance Raman spectroscopy is a powerful technique for probing the structure and formation mechanism of protein fibrils, which are traditionally difficult to study with other techniques owing to their low solubility and noncrystalline arrangement. Utilizing a tunable deep UV Raman system allows for selective enhancement of different chromophores in protein fibrils, which provides detailed information on different aspects of the fibrils' structure and formation. Additional information can be extracted with the use of advanced data treatment such as chemometrics and 2D correlation spectroscopy. In this chapter we give an overview of several techniques for utilizing deep UV resonance Raman spectroscopy to study the structure and mechanism of formation of protein fibrils. Clever use of hydrogen-deuterium exchange can elucidate the structure of the fibril core. Selective enhancement of aromatic amino acid side chains provides information about the local environment and protein tertiary structure. The mechanism of protein fibril formation can be investigated with kinetic experiments and advanced chemometrics. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 6 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 2 | 33% |
| Student > Bachelor | 1 | 17% |
| Professor | 1 | 17% |
| Unknown | 2 | 33% |
| Readers by discipline | Count | As % |
|---|---|---|
| Chemistry | 3 | 50% |
| Materials Science | 1 | 17% |
| Unknown | 2 | 33% |