The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts

Protein Science

Volumn 20, Issue 12, 2011, Pages 2023-2034

  Kjaergaard, Magnus ^a   Iešmantavičius, Vytautas ^a   Poulsen, Flemming M ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Aliphatic side chains; Conformational ensemble; Denatured state; Hydrophobic packing; Intrinsically disordered proteins; Natively unfolded proteins

Indexed keywords

CARBON 13; ISOLEUCINE; LEUCINE; PROTEIN; RETINOID X RECEPTOR; THYROID HORMONE; TRIFLUOROETHANOL; VALINE;

ALPHA HELIX; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; HYDROPHOBICITY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN INDUCTION; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; QUANTITATIVE ANALYSIS;

ANIMALS; CATTLE; DIAZEPAM BINDING INHIBITOR; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEAR RECEPTOR COACTIVATOR 3; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN UNFOLDING; PROTEINS;

EID: 81755161591     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.726     Document Type: Article

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