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Cold‐ and Pressure‐Induced Dissociation of Protein Aggregates and Amyloid Fibrils
Author(s) -
Mishra Rajesh,
Winter Roland
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200802027
Subject(s) - amyloid fibril , dissociation (chemistry) , fibril , biophysics , chemistry , protein aggregation , amyloid (mycology) , amyloid β , biochemistry , biology , medicine , organic chemistry , inorganic chemistry , disease
Cold denaturation (including supercooling) and pressure perturbation are able to dissolve protein aggregates and, in some cases, amyloid fibrils (see picture). These studies provide additional details on the polymorphic forms of amyloid structures and their precursors as well as the transformation processes between polymorphic states.