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Solid state nuclear magnetic resonance v.88, 2017년, pp.1 - 14   SCI SCIE
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Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy

van der Wel, Patrick C.A.
  • 초록  

    Abstract The aggregation of proteins and peptides into a variety of insoluble, and often non-native, aggregated states plays a central role in many devastating diseases. Analogous processes undermine the efficacy of polypeptide-based biological pharmaceuticals, but are also being leveraged in the design of biologically inspired self-assembling materials. This Trends article surveys the essential contributions made by recent solid-state NMR (ssNMR) studies to our understanding of the structural features of polypeptide aggregates, and how such findings are informing our thinking about the molecular mechanisms of misfolding and aggregation. A central focus is on disease-related amyloid fibrils and oligomers involved in neurodegenerative diseases such as Alzheimer's, Parkinson's and Huntington's disease. SSNMR-enabled structural and dynamics-based findings are surveyed, along with a number of resulting emerging themes that appear common to different amyloidogenic proteins, such as their compact alternating short-β-strand/β-arc amyloid core architecture. Concepts, methods, future prospects and challenges are discussed. Highlights The aggregation of peptides and proteins is a hallmark of many incurable diseases. Solid-state NMR site-specifically probes the conformation of protein aggregates. Solid-state NMR studies of dynamics and disordered regions yield unique insights. Recent solid-state NMR structures point to common molecular themes and mechanisms. Graphical abstract [DISPLAY OMISSION]


  • 주제어

    Amyloid .   Neurodegenerative disease .   Magic-angle spinning .   Protein structure .   Protein dynamics .   Protein misfolding .   Structural biology .   Prions.  

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