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- Title
Glimpses of the molecular mechanisms of β<sub>2</sub>-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape
- Authors
Platt, Geoffrey W.; Radford, Sheena E.
- Abstract
Abstract: β2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanisms of fibril formation from a full-length protein in vitro. Fibrils have been assembled from β2m under both low pH conditions, where the precursor is disordered, and at neutral pH where the protein is initially natively folded. Here we discuss the roles of sequence and structure in amyloid formation, the current understanding of the structural mechanisms of the early stages of aggregation of β2m at both low and neutral pH, and the common and distinct features of these assembly pathways.
- Subjects
GLOBULINS; FIBERS; CELL aggregation; NUCLEAR magnetic resonance; AMYLOID; DIALYSIS (Chemistry); AMYLOIDOSIS; PROTEIN structure
- Publication
FEBS Letters, 2009, Vol 583, Issue 16, p2623
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.05.005