Easy and unambiguous sequential assignments of intrinsically disordered proteins by correlating the backbone 15N or 13C' chemical shifts of multiple contiguous residues in highly resolved 3D spectra

Journal of Biomolecular NMR

Volumn 61, Issue 2, 2015, Pages 109-121

  Yoshimura, Yuichi ^a   Kulminskaya, Natalia V ^a   Mulder, Frans A A ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

Carbonyl carbonyl J coupling; Chemical shift degeneracy; Homonuclear isotropic mixing; Intrinsically disordered proteins; Sequential resonance assignment

Indexed keywords

AMIDE; CARBONYL DERIVATIVE; INTRINSICALLY DISORDERED PROTEIN; NITROGEN; PROLINE; CARBON;

ANALYTIC METHOD; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CHEMICAL BOND; NITROGEN NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN UNFOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; THREE DIMENSIONAL IMAGING; CHEMISTRY; NUCLEAR MAGNETIC RESONANCE; PROCEDURES; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

CARBON ISOTOPES; CARBON-13 MAGNETIC RESONANCE SPECTROSCOPY; INTRINSICALLY DISORDERED PROTEINS; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 84923349518     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-014-9890-7     Document Type: Article

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