Bacterial amyloid fibrils

Jarrett JT, Lansbury PT Jr. Amyloid fibril formation requires a chemically discriminating nucleation event studies of an amyloidogenic sequence from the bacterial protein OsmB. Biochemistry 1992 31 12345-12352. 

Hong et al. discussed recent advances in using SSNMR to study K and H" " channels, Ca + pumps, G protein-coupled receptors, bacterial outer membrane proteins, and viral fusion proteins to elucidate their mechanisms of action at the membrane. Shi and Ladizhansky underlined that SSNMR has become a prominent method for the characterization of insoluble proteins and protein aggregates such as amyloid fibrils and membrane-lipid complexes. Im et al. developed SSNMR ensemble dynamics (SSNMR-ED) using multiple conformer models, which generates an ensemble of structures that satisfies the experimental observables without any fitting parameters. 

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