Myoglobin fibrils

Fandrich, M., Fletcher, M. A., and Dobson, C. M. (2001). Amyloid fibrils from muscle myoglobin—Even an ordinary globular protein can assume a rogue guise if conditions are right. Nature 410, 165-166. 

Fandrich, M., Forge, V., Buder, K., Kittler, M., Dobson, C. M., and Diekmann, S. (2003). Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proc. Natl. Acad. Sci. USA 100, 15463-15468. 

Figure 23-3 Infrared absorbance spectra of the amide regions of proteins. (A) Spectra of insulin fibrils illustrating dichroism. Solid line, electric vector parallel to fibril axis broken line, electric vector perpendicular to fibril axis. From Burke and Rougvie.24 Courtesy of Malcolm Rougvie. See also Box 29-E. (B) Fourier transform infrared (FTIR) spectra of two soluble proteins in aqueous solution obtained after subtraction of the background H20 absorption. The spectrum of myoglobin, a predominantly a-helical protein, is shown as a continuous line. That of concanavalin A, a predominantly (3-sheet containing protein, is shown as a broken line. From Haris and Chapman.14 Courtesy of Dennis Chapman.

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