Adiabatically swept pulses were originally designed for the purpose of broadband spin inversion. Later, unexpected advantages of their utilization were also found in other applications, such as refocusing to excite spin echoes, studies of chemical exchange or fragment-based drug design. Here, we present new experiments to characterize fast (ps-ns) protein dynamics, which benefit from little-known properties of adiabatic pulses. We developed a strategy for measuring cross-correlated cross-relaxation (CCCR) rates during adiabatic pulses. This experiment provides a linear combination of longitudinal and transverse CCCR rates, which is offset-independent across a typical amide (15)N spectrum. The pulse sequence can be recast to provide accurate transverse CCCR rates weighted by the populations of exchanging states. Sensitivity can be improved in systems in slow exchange. Finally, the experiments can be easily modified to yield residue-specific correlation times. The average correlation time of motions can be determined with a single experiment while at least two different experiments had to be recorded until now.

Central European Institute of Technology Masaryk University Kamenice 5 625 00 Brno Czech Republic

École Normale Supérieure PSL Research University Département de Chimie 24 rue Lhomond 75005 Paris France

Institut des Sciences et Ingénierie Chimiques École polytechnique fédérale de Lausanne 1015 Lausanne Switzerland

Institute of Organic Chemistry Center for Molecular Biosciences Innsbruck University of Innsbruck Innrain 80 82 6020 Innsbruck Austria

National Centre for Biomolecular Research Faculty of Science Masaryk University Kamenice 5 625 00 Brno Czech Republic

Sorbonne Universités UPMC Univ Paris 06 LBM 4 place Jussieu 75005 Paris France

UMR 7203 LBM CNRS 75005 Paris France

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