Kinetics and thermodynamics of amyloid fibril assembly
Article Abstract:
A research was conducted to prove the possibility to derive kinetics and thermodynamics information on aggregation that can be explained with respect to details of aggregate structure and assembly mechanisms in the standard technique for globular protein folding studies. The observations from the study of the well-behaved amyloid system provide a new angle to the assembly pathways and the structures of off-pathway aggregates and new clues to pathology.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
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Direct observation of amyloid fibril growth, propagation, and adaptation
Article Abstract:
Amyloid fibrils are created through nucleation and growth, various investigations are done to understand the mechanism involved and feature of each process of nucleation, growth, propagation and adaptation at single fibrillar level are described. The direct observations show that template-dependent growth and structural diversity are the main reasons in deciding the structure and the role of the amyloid fibrils.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
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Monitoring protein folding at atomic resolution
Article Abstract:
The recent applications of nuclear magnetic resonance spectroscopy to monitor protein folding/unfolding reactions at atomic resolution are discussed. NMR will play a pivotal role in the characterization of dynamic systems and will be technique of choice to investigate the kinetics of protein folding/unfolding at the residue level.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2004
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