Protein structure determination by magic-angle spinning solid-state NMR, and insights into the formation, structure, and stability of amyloid fibrils

Annual Review of Biophysics

Volumn 42, Issue 1, 2013, Pages 515-536

  Comellas, Gemma ^a   Rienstra, Chad M ^a,b  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b Department of Chemistry ^*  (United States)

Author keywords

computational advances; dynamic nuclear polarization; electron microscopy; high resolution; pulse sequences; structural restraints

Indexed keywords

ALPHA DEFENSIN; AMANTADINE; AMYLOID BETA PROTEIN; AMYLOID PROTEIN; HUNTINGTIN; KALIOTOXIN; MASTOPARAN; SPECTRIN; UBIQUITIN;

ALZHEIMER DISEASE; ARTICLE; BETA SHEET; BIOTRANSFORMATION; FAMILIAL AMYLOID POLYNEUROPATHY; MAGNETIC FIELD; MOLECULAR DYNAMICS; NON INSULIN DEPENDENT DIABETES MELLITUS; NUCLEAR MAGNETIC RESONANCE; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DATA BANK; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; SPECTROSCOPY; STRUCTURE ACTIVITY RELATION; VASCULAR AMYLOIDOSIS;

AMYLOID; ANIMALS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY;

EID: 84877746282     PISSN: 1936122X     EISSN: 19361238     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-083012-130356     Document Type: Article

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