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Default Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.

Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.

Related Articles Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.

Annu Rev Biophys. 2013 Mar 22;

Authors: Comellas G, Rienstra CM

Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable development in the past decade. Significant advances in instrumentation, sample preparation, spectroscopic techniques, and computational methods have made possible the determination of the first high-resolution structures of a peptide and a protein in 2002. Subsequent developments allowed the investigation of larger proteins, the initial application of automated analysis routines, and substantial improvements in structural resolution. The application of these methods has enabled the investigation of amyloid fibril structures, conformational dynamics, and their assembly pathways at an atomic level for the first time, as these are systems not accessible by other common techniques. Recent advances and future trends for protein structure determination using MAS SSNMR, as well as their application to the study of amyloid fibrils, are reviewed. Expected final online publication date for the Annual Review of Biophysics Volume 42 is May 06, 2013. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.


PMID: 23527778 [PubMed - as supplied by publisher]



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