Site-Specific ?- and ?-Torsion Angle Determination in a Uniformly/Extensively 13C- and 15N-Labeled Peptide
 

Site-Specific ?- and ?-Torsion Angle Determination in a Uniformly/Extensively 13C- and 15N-Labeled Peptide


Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 17 August 2011</br>
Sungsool, Wi , Justin, Spano</br>
A solid-state rotational-echo double resonance (REDOR) NMR method was introduced to identify the ?- and ?-torsion angle from a 1H–15N or 1H–13C? spin system of alanine-like residues in a selectively, uniformly, or extensively 15N-/13C-labeled peptide. When a C?(i) or a 15N peak is site-specifically obtainable in the NMR spectrum of a uniformly 15N/13C-labeled sample system, the ?- or ?-torsion angle specified by the conformational structure of peptide geometry involving 15N(i)–1H?(i)–15N(i+1) or 13C?(i-1)–1HN(i)–13C?(i) spin system can be identified based on 13C?- or 15N-detected 1H?–15N or 1HN–13C REDOR experiment. This method will conveniently be utilized to identify major secondary motifs, such as...</br>
Graphical abstract

*Graphical abstract:**Highlights:*? Determination of ?- and ?-torsion angles of a uniformly 13C-/15N-labeled peptide. ? Rotational-echo double resonance (REDOR) NMR. ? Tri-spin systems, 15N(i)-1H?(i)-15N(i+1) and 13C?(i-1)-1HN(i)-13C?(i).
http://www.sciencedirect.com/cache/M...JX-53K00F9-1-2</br></br>

Source: Journal of Magnetic Resonance