Premium
Inside Back Cover: A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid β (1 – 40) (ChemPhysChem 17/2016)
Author(s) -
Adler Juliane,
Baumann Monika,
Voigt Bruno,
Scheidt Holger A.,
Bhowmik Debanjan,
Häupl Tilmann,
Abel Bernd,
Madhu Perunthiruthy K.,
Balbach Jochen,
Maiti Sudipta,
Huster Daniel
Publication year - 2016
Publication title -
chemphyschem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201600880
Subject(s) - amyloid fibril , cover (algebra) , fibril , amyloid (mycology) , chemistry , morphology (biology) , biophysics , molecular dynamics , fibrillation , kinetics , amyloid β , crystallography , nanotechnology , materials science , biochemistry , computational chemistry , biology , physics , engineering , genetics , medicine , mechanical engineering , inorganic chemistry , disease , pathology , quantum mechanics , cardiology , atrial fibrillation
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. on page 2744 in Issue 17, 2016 (DOI: 10.1002/cphc.201600413).