Ontology highlight
ABSTRACT:
SUBMITTER: Dhulesia A
PROVIDER: S-EPMC2974344 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
Dhulesia Anne A Cremades Nunilo N Kumita Janet R JR Hsu Shang-Te Danny ST Mossuto Maria F MF Dumoulin Mireille M Nietlispach Daniel D Akke Mikael M Salvatella Xavier X Dobson Christopher M CM
Journal of the American Chemical Society 20101101 44
The partial unfolding of human lysozyme underlies its conversion from the soluble state into amyloid fibrils observed in a fatal hereditary form of systemic amyloidosis. To understand the molecular origins of the disease, it is critical to characterize the structural and physicochemical properties of the amyloidogenic states of the protein. Here we provide a high-resolution view of the unfolding process at low pH for three different lysozyme variants, the wild-type protein and the mutants I56T a ...[more]