TROSY for Studies of Dynamic Processes

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In addition to structural data, NMR is able to provide information on dynamic processes at atomic resolution over a wide range of time scales (Kay et al. 1989; Palmer 2004), which potentially can help understanding structure and function relationships (Mulder et al. 2001; Eisenmesser et al. 2002). Key experiments for dynamic studies measure Ti and T2 relaxation times and heteronuclear 15N{1H} NOEs of the 15N nuclei in amide groups. For these important experiments, pulse sequence using [15N,1H]-TROSY were developed (Zhu et al. 2000). Recently, these experiments were extended to three dimensions based on a 3D TROSY-HNCO sequence, which can be applied to resolve signal overlap in the 2D spectra (Xia et al. 2002). Please note that TROSY does not change the 15N-spin relaxation parameters typically measured. A few examples of the application of [15N,1H]-TROSY experiments for the study of protein dynamics are given in Sect. 5.5.

Not only the [15N,1H]-TROSY effect can be used to obtain relaxation data, but also the methyl TROSY effect. Recently, a new experiment based on methyl-TROSY was proposed for studies of slow (millisecond) dynamic processes in high molecular mass proteins (Korzhnev et al. 2004) and was demonstrated with the 82 kDa enzyme malate synthase G, where the new approach resulted in a sensitivity gain of a factor of 5.

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