Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis 1 1Edited by F. E. Cohen
- 1 March 2000
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 296 (4) , 961-968
- https://doi.org/10.1006/jmbi.2000.3514
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Water-Soluble β-Sheet Models Which Self-Assemble into Fibrillar StructuresBiochemistry, 1999
- Engineering of betabellin-15d: A 64 residue beta sheet protein that forms long narrow multimeric fibrilsProtein Science, 1998
- De novo heme proteins from designed combinatorial librariesProtein Science, 1997
- A Protein Designed by Binary Patterning of Polar and Nonpolar Amino Acids Displays Native-like PropertiesJournal of the American Chemical Society, 1997
- Transthyretin Quaternary and Tertiary Structural Changes Facilitate Misassembly into AmyloidPublished by Elsevier ,1997
- Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteinsProtein Science, 1995
- Protein Design by Binary Patterning of Polar and Nonpolar Amino AcidsScience, 1993
- Favored and suppressed patterns of hydrophobic and nonhydrophobic amino acids in protein sequences.Proceedings of the National Academy of Sciences, 1993
- Identification of protein folds: Matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structuresProteins-Structure Function and Bioinformatics, 1990
- β structures of alternating polypeptides and their possible prebiotic significanceNature, 1975