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Conversion of yeast phosphoglycerate kinase into amyloid-like structure

Item Type:Article
Title:Conversion of yeast phosphoglycerate kinase into amyloid-like structure
Creators Name:Damaschun, G. and Damaschun, H. and Fabian, H. and Gast, K. and Kroeber, R. and Wieske, M. and Zirwer, D.
Abstract:Yeast phosphoglycerate kinase is a structurally well-characterized enzyme consisting of 415 amino acids without disulfide bonds. Anion-induced 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 x 5.1 nm. About half of all amino acids are organized in form of cross-β 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-{beta} structure practically comes to an end already after some hours, whereas the length-growth of the amyloid fibrils, monitored by small-angle X-ray scattering, was not yet completed after 1,300 hours.
Keywords:Amyloid, Dynamic Light Scattering, Electron Microscopy, Fibrillogenesis, Infrared Spectroscopy, Misfolding, Phosphoglycerate Kinase, Protein Folding, X-ray Scattering
Source:Proteins: Structure, Function, and Bioinformatics
ISSN:0887-3585
Publisher:Wiley (U.S.A.)
Volume:39
Number:3
Page Range:204-211
Date:15 May 2000
Official Publication:https://doi.org/10.1002/(SICI)1097-0134(20000515)39:3<204::AID-PROT20>3.0.CO;2-8
PubMed:View item in PubMed

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