Inside Back Cover: A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid β (1–40) (ChemPhysChem 17/2016). Issue 17 (5th September 2016)

• Record Type: Journal Article
• Authors: Adler, Juliane; Baumann, Monika; Voigt, Bruno; Scheidt, Holger A.; Bhowmik, Debanjan; Häupl, Tilmann; Abel, Bernd; Madhu, Perunthiruthy K.; Balbach, Jochen; Maiti, Sudipta; Huster, Daniel
• Is Part Of: Chemphyschem. Volume 17:Issue 17(2016)
• Page Start: 2773
• Page End: 2773
• Publication Date: 2016-09-05
• Subjects: amyloids -- fibrils -- mutagenesis -- NMR spectroscopy -- peptides; Chemistry, Physical and theoretical -- Periodicals; 541.05
• DOI: 10.1002/cphc.201600880
• Languages: English
• ISSNs: 1439-4235

Abstract

Abstract : The Inside Back Cover summarizes the strategy applied to study the influence of local physical forces on the fibrillation kinetics, structure, and dynamics of amyloid β (1–40) fibrils. Rationally designed mutations were introduced to modify the hydrophobic contact between residues 19 and 34. More information can be found in the Full Paper by J. Adler et al. onpage 2744 in Issue 17, 2016 (DOI:10.1002/cphc.201600413 ).