Exclusion of the Native α-Helix from the Amyloid Fibrils of a Mixed α/β Protein

Protein aggregation in bacteria: the thin boundary between functionality and toxicity

“…However under atomic force microscopy, IBs appear amorphous. This observation does not dismiss the fact that IBs might indeed have an amyloid structure, because even amyloids do not incorporate their entire polypeptide length into the highly packed b-sheet structure as seen in yeast prions (Morgan et al, 2008). The secondary structure content analysis of IBs confirmed that there are fibrillar and nonfibrillar regions included (Balguerie et al, 2003).…”

Limited Proteolysis Reveals That Amyloids from the 3D Domain-Swapping Cystatin B Have a Non-Native β-Sheet Topology

“…this form of the protein is favoured thermodynamically [25][26][27]. Discovery of this phenomenon in cystatin C provided the first observation of 3D-domain swapping in a recognised amyloidogenic protein.…”

Structure and Function of Stefin B Oligomers – Important Role in Amyloidogenesis

“…Following changes during the lag phase of the reaction by SEC and ESI MS we were able to improve the model of amyloid fibril formation (Figure 4), further explaining the role of various off-pathway oligomers [41]. Dimers seem to be the building block from which fibril formation starts and the fibrils grow [56]. When the process was started from any kind of oligomers, these transformed into dimers [41].…”

“…Crystal or solution structure of stefin B monomer and oligomers have been so far characterized from monomer in complex with the target enzyme [54], dimer under amyloid forming conditions [55], tetramer [40] to model of amyloid fibrils [56]. Domain-swapped dimer of stefin A has also been determined by heteronuclear NMR [57].…”

“…The structured core of human stefin B amyloid fibrils has been determined ( Figure 3C) [56]. Based on the H/D exchange rates the structure could be divided onto protected region (inside the fibril core) and unprotected region (striking out of the fibril).…”