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.
Yoshimura, Yuichi
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. [electronic resource] - Journal of biomolecular NMR Feb 2015 - 109-21 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1573-5001
10.1007/s10858-014-9890-7 doi
Carbon Isotopes--chemistry
Carbon-13 Magnetic Resonance Spectroscopy--methods
Intrinsically Disordered Proteins--analysis
Nitrogen Isotopes--chemistry
Nuclear Magnetic Resonance, Biomolecular--methods
Protein Conformation
Protein Structure, Secondary
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. [electronic resource] - Journal of biomolecular NMR Feb 2015 - 109-21 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1573-5001
10.1007/s10858-014-9890-7 doi
Carbon Isotopes--chemistry
Carbon-13 Magnetic Resonance Spectroscopy--methods
Intrinsically Disordered Proteins--analysis
Nitrogen Isotopes--chemistry
Nuclear Magnetic Resonance, Biomolecular--methods
Protein Conformation
Protein Structure, Secondary