Distance information for disordered proteins from NMR and ESR measurements using paramagnetic spin labels

Methods in Molecular Biology

Volumn 895, Issue , 2012, Pages 127-138

  Eliezer, David ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

Author keywords

Denatured state; ESR; Intrinsically unstructured; Natively unfolded; NMR; Paramagnetic relaxation enhancement; Pulsed dipolar spectroscopy; Random coil; Unfolded state

Indexed keywords

SYNUCLEIN;

ARTICLE; CHEMISTRY; ELECTRON SPIN RESONANCE; GENETICS; HUMAN; MISSENSE MUTATION; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN UNFOLDING; QUANTUM THEORY; STAINING;

ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; MUTATION, MISSENSE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN UNFOLDING; QUANTUM THEORY; STAINING AND LABELING; SYNUCLEINS;

EID: 84865326807     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-927-3_10     Document Type: Article

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