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A flash in the pan: Dissecting dynamic amyloid intermediates using fluorescence
Author(s) -
Nath Abhinav,
Rhoades Elizabeth
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.02.044
Subject(s) - amyloid (mycology) , chemistry , amyloid fibril , protein aggregation , fluorescence , biophysics , fluorescence correlation spectroscopy , biochemistry , computational biology , amyloid β , biology , molecule , medicine , inorganic chemistry , physics , disease , organic chemistry , pathology , quantum mechanics
Several widespread and severe degenerative diseases are characterized by the deposition of amyloid protein aggregates in affected tissues. While there is great interest in the complete description of the aggregation pathway of the proteins involved, a molecular level understanding is hindered by the complexity of the self‐assembly process. In particular, the early stages of aggregation, where dynamic, heterogeneous and often toxic intermediates are populated, are resistant to high‐resolution structural characterization. Fluorescence spectroscopy is a powerful and versatile tool for such analysis. In this review, we survey its application to provide residue‐specific information about amyloid intermediate states for three selected proteins: IAPP, α‐synuclein, and tau.