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Understanding the complex mechanisms of β 2 ‐microglobulin amyloid assembly
Author(s) -
Eichner Timo,
Radford Sheena E.
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08186.x
Subject(s) - amyloid (mycology) , beta 2 microglobulin , protein folding , amyloid fibril , amyloidosis , protein aggregation , folding (dsp implementation) , amyloid disease , chemistry , in vitro , in vivo , biophysics , computational biology , biochemistry , biology , amyloid β , disease , medicine , immunology , pathology , inorganic chemistry , microbiology and biotechnology , electrical engineering , engineering
Several protein misfolding diseases are associated with the conversion of native proteins into ordered protein aggregates known as amyloid. Studies of amyloid assemblies have indicated that non‐native proteins are responsible for initiating aggregation in vitro and in vivo . Despite the importance of these species for understanding amyloid disease, the structural and dynamic features of amyloidogenic intermediates and the molecular details of how they aggregate remain elusive. This review focuses on recent advances in developing a molecular description of the folding and aggregation mechanisms of the human amyloidogenic protein β 2 ‐microglobulin under physiologically relevant conditions. In particular, the structural and dynamic properties of the non‐native folding intermediate I T and its role in the initiation of fibrillation and the development of dialysis‐related amyloidosis are discussed.