Conversion of yeast phosphoglycerate kinase into amyloid-like structure

✍ Scribed by Gregor Damaschun; Hilde Damaschun; Heinz Fabian; Klaus Gast; Reinhard Kröber; Martin Wieske; Dietrich Zirwer

• Book ID: 101227604
• Publisher: John Wiley and Sons
• Year: 2000
• Tongue: English
• Weight: 216 KB
• Volume: 39
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(20000515)39:3<204::aid-prot20>3.0.co;2-8

✦ Synopsis

Yeast phosphoglycerate kinase is a structurally well-characterized enzyme consisting of 415 amino acids without disulfide bonds. Anioninduced refolding from its acid-unfolded state gives rise to the formation of worm-like amyloid fibrils with a persistence length of 73 nm. Electron microscopy and small-angle X-ray scattering data indicate that the fibrils have an elliptical cross-section with dimensions of 10.2 nm ؋ 5.1 nm. About half of all amino acids are organized in form of cross-␤ structure which gives rise to typical infrared spectra, X-ray diffraction and yellow-green birefringence after Congo red staining. The kinetics of amyloid formation, monitored by infrared spectroscopy, dynamic light scattering and X-ray scattering, was found to be strongly dependent on protein concentration. The infrared data indicate that the formation of cross-␤ structure practically comes to an end already after some hours, whereas the lengthgrowth of the amyloid fibrils, monitored by smallangle X-ray scattering, was not yet completed after 1,300 hours. Proteins 2000;39:204 -211.