Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
Top Cited Papers
- 9 December 2003
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 100 (26) , 15463-15468
- https://doi.org/10.1073/pnas.0303758100
Abstract
Observations that β-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed β-structure or by association of unfolded polypeptide segments. By using α-helical protein apomyoglobin, we show that the ease of fibril assembly correlates with the extent of denaturation. By contrast, monomeric β-sheet intermediates could not be observed under the conditions of fibril formation. These data suggest that amyloid fibril formation from apomyoglobin depends on disordered polypeptide segments and conditions that are selectively unfavorable to folding. However, it is inevitable that such conditions often stabilize protein folding intermediates.Keywords
This publication has 39 references indexed in Scilit:
- Dependence on solution conditions of aggregation and amyloid formation by an SH3 domainJournal of Molecular Biology, 2001
- Protein engineering as a strategy to avoid formation of amyloid fibrilsProtein Science, 2000
- Transthyretin Quaternary and Tertiary Structural Changes Facilitate Misassembly into AmyloidPublished by Elsevier ,1997
- Analysis of Main Chain Torsion Angles in Proteins: Prediction of NMR Coupling Constants for Native and Random Coil ConformationsJournal of Molecular Biology, 1996
- Pressure-Induced Perturbation of Apomyoglobin Structure: Fluorescence Studies on Native and Acidic Compact FormsBiochemistry, 1996
- Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helixes of myoglobinBiochemistry, 1993
- Sequential mechanism of refolding of carbonic anhydrase BFEBS Letters, 1987
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969
- The Role of Dipole Interactions in Determining Polypeptide ConfigurationsJournal of the American Chemical Society, 1965
- Cleavage of the haem-protein link by acid methylethylketoneBiochimica et Biophysica Acta, 1959