Triple resonance three-dimensional protein NMR: Before it became a black box
 

Triple resonance three-dimensional protein NMR: Before it became a black box


Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Corrected Proof, Available online 31 August 2011</br>
Ad, Bax</br>
Three-dimensional triple resonance experiments have become an integral part of virtually every solution NMR study of proteins. The approach relies on uniform isotopic enrichment of proteins with 13C and 15N, and establishes the scalar connectivity pathway between nuclei through the large 1JNH, 1JCH, 1JCC, and 1JCN couplings. The magnetization transfer process takes place through multiple, efficient one-bond magnetization transfer steps, rather than a single step through the smaller and variable 3JHH couplings. The relatively large size and good uniformity of the one-bond couplings allowed the design of efficient magnetization transfer schemes that are effectively uniform across a given protein, nearly...</br>

Source: Journal of Magnetic Resonance