Long Time Dynamic Simulations: Exploring the Folding Pathways of an Alzheimer's Amyloid Aβ-Peptide
Accounts of Chemical Research2002Vol. 35(6), pp. 473–481
Citations Over TimeTop 10% of 2002 papers
Abstract
We describe the MaxFlux algorithm for the computation of likely pathways for global macromolecular conformational transitions. The algorithm assumes an overdamped diffusive dynamics for the biomolecule, appropriate to large scale conformational changes. As an application of the MaxFlux method, we explore conformational transitions between alpha-helical, collapsed coil, and beta-sheet conformations of an amyloid Abeta-peptide. The resulting transition pathways are analyzed in terms of the mechanism of conformational transition and the progression of the peptide energetics in both an aqueous and a membrane-mimicking nonpolar solvent.
Related Papers
- → Stretching-Induced Conformational Transition of the Crystalline and Noncrystalline Domains of 13C-Labeled Bombyx mori Silk Fibroin Monitored by Solid State NMR(2015)37 cited
- → Reshaping the Protein Folding Pathway by Osmolyte via its Effects on the Folding Intermediates(2015)10 cited
- → Comparing the Folding and Misfolding Energy Landscapes of Phosphoglycerate Kinase(2012)7 cited
- The Conformational Transition of Regenerated Silk Fibroin Aqueous Solution Durng the Storage(2006)
- → Circular Dichroism of Biomolecules(2011)