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Inside Cover: Significant Structural Differences between Transient Amyloid‐β Oligomers and Less‐Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations (Angew. Chem. Int. Ed. 27/2014)
Author(s) -
Sarkar Bidyut,
Mithu Venus Singh,
Chandra Bappaditya,
Mandal Arghya,
Chandrakesan Muralidharan,
Bhowmik Debanjan,
Madhu Perunthiruthy K.,
Maiti Sudipta
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201405438
Subject(s) - cover (algebra) , fibril , amyloid (mycology) , amyloid fibril , aggregate (composite) , int , nuclear magnetic resonance spectroscopy , biophysics , spectroscopy , membrane , amyloid β , solid state nuclear magnetic resonance , chemistry , crystallography , materials science , biochemistry , stereochemistry , biology , nanotechnology , nuclear magnetic resonance , pathology , computer science , medicine , operating system , mechanical engineering , inorganic chemistry , physics , disease , quantum mechanics , engineering
The molecular structure of a rapidly changing protein aggregate is deciphered by P. K. Madhu, S. Maiti et al. in their Communication on page 6888 ff. An aggregating amyloid beta solution is added dropwise into liquid nitrogen. This freezes a particular state of the evolving aggregate (blue droplet), which has a high affinity for cell membranes (microscopy image). The structural parameters of this state are determined by solid‐state NMR spectroscopy of the lyophilized frozen solution.