Reversible Random Coil to β-Sheet Transition and the Early Stage of Aggregation of the Aβ(12−28) Fragment from the Alzheimer Peptide
- 20 April 2000
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (18) , 4261-4268
- https://doi.org/10.1021/ja991167z
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Aqueous Dissolution of Alzheimer's Disease Aβ Amyloid Deposits by Biometal DepletionJournal of Biological Chemistry, 1999
- Assembly of Aβ Amyloid Protofibrils: An in Vitro Model for a Possible Early Event in Alzheimer's DiseaseBiochemistry, 1999
- Amyloid β-peptide polymerization studied using fluorescence correlation spectroscopyChemistry & Biology, 1999
- Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer’s disease 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- Amyloid β-Protein FibrillogenesisJournal of Biological Chemistry, 1997
- Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's diseaseJournal of Molecular Biology, 1992
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's diseaseJournal of Molecular Biology, 1991
- Limiting equivalent conductance of perchloric acid in 0.9914 mole fraction N-methylacetamide (NMA) at 40.deg.The Journal of Physical Chemistry, 1973
- Computed circular dichroism spectra for the evaluation of protein conformationBiochemistry, 1969