Abstract
Mass spectrometry has become increasingly important in amyloid research specifically in the mechanism of formation and characterization of fibrils. In this review we highlight key experiments that provide evidence for different conformations, interactions and unfolding intermediates in proteins associated with amyloid diseases.
Keywords: Mass spectrometry, amyloidogenic, hydrogen exchange, protein conformation
Protein & Peptide Letters
Title: Insights into Amyloid Fibril Formation from Mass Spectrometry
Volume: 13 Issue: 3
Author(s): Gemma L. Caddy and Carol V. Robinson
Affiliation:
Keywords: Mass spectrometry, amyloidogenic, hydrogen exchange, protein conformation
Abstract: Mass spectrometry has become increasingly important in amyloid research specifically in the mechanism of formation and characterization of fibrils. In this review we highlight key experiments that provide evidence for different conformations, interactions and unfolding intermediates in proteins associated with amyloid diseases.
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Cite this article as:
Caddy L. Gemma and Robinson V. Carol, Insights into Amyloid Fibril Formation from Mass Spectrometry, Protein & Peptide Letters 2006; 13 (3) . https://dx.doi.org/10.2174/092986606775338416
DOI https://dx.doi.org/10.2174/092986606775338416 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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