作者: I. Segers-Nolten , M. van Raaij , V. Subramaniam
DOI: 10.1016/B978-0-08-100691-7.00155-5
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摘要: Amyloid formation is a fascinating process with both biomedical and materials science relevance. Amyloids can be pathological, but also possess interesting potential for use as nanobiomaterials. Although amyloids have long been the focus of intense study, amyloid mechanism stays unclear, including factors that initiate drive aggregation process. This chapter describes application advanced biophysical methods, such (single-molecule) fluorescence spectroscopy, electron paramagnetic resonance (EPR) circular dichroism (CD) high-resolution atomic force microscopy (AFM), exploration characteristics. Collectively, selection techniques provides access to all stages aggregation: from monomers oligomeric intermediates, mature fibrils. Single-molecule shown provide information on monomer structure flexibility. On an ensemble level, conformational acquired using CD spectroscopy EPR spectroscopy. High-resolution AFM enables detailed morphological mechanical properties fibrillar structures. The research approaches described are widely applicable broader genre proteins uncover mysteries underlie complex biophysics their optimal utilization in bionanotechnology.