Conformational change and assembly through edge [beta] strands in transthyretin and other amyloid proteins
Article Abstract:
The amyloid protein transthyretin technique provides an outstanding set up for analyzing the conformational changes and the resulting subunit-subunit associations that result in formation of insoluble, amyloid protein fibrils associated with various deadly diseases. A working model for transthyretin amyloid is described, which reveals an 'unprotected' edge [beta] strand and afterwards the symmetric assembly of subunits to head-to-head and tail-to-tail protofibrils and also show the relations to various amyloid systems.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
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The aggregation and fibrillation of [alpha]-synuclein
Article Abstract:
The aggregation of the small, ample, essentially disordered presynaptic protein [alpha]-synuclein is supposed to be a significant step in Parkinson's disease. The detailed examination into the molecular basis for [alpha]-synuclein aggregation/fibrillation along with the factors that increase or hamper fibrillation, effects of molecular crowding, oxidation, point mutations, and lipid membranes, and different conformational and oligomeric states adopted by [alpha]-synuclein is presented.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
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Exploring the early steps of amyloid peptide aggregation by computers
Article Abstract:
The structural and dynamic aspects of the aggregation as observed in state-of-the-art computer simulations of amyloid-forming peptides are studied with an emphasis on the activation-relaxation technique (ART). It is concluded that numerical methods, including ART- optimized potential for efficient peptide-structure prediction (OPEP) is playing a central role in proposing structural and dynamic information.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2005
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