Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins.
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.
École Normale Supérieure - PSL Research University, Département de Chimie, 24 rue Lhomond, 75005, Paris, France.|Sorbonne Universités UPMC Univ Paris 06, LBM, 4 place Jussieu, 75005, Paris, France.|UMR 7203 LBM, CNRS, 75005, Paris, France.|National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.|Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.|Institut des Sciences et Ingénierie Chimiques, École polytechnique fédérale de Lausanne, 1015, Lausanne, Switzerland.
Pavel
P
Kadeřávek
Institute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.
Sarina
S
Grutsch
Institut des Sciences et Ingénierie Chimiques, École polytechnique fédérale de Lausanne, 1015, Lausanne, Switzerland.
Nicola
N
Salvi
Institute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.
Martin
M
Tollinger
National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.|Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.
Lukáš
L
Žídek
École Normale Supérieure - PSL Research University, Département de Chimie, 24 rue Lhomond, 75005, Paris, France.|Sorbonne Universités UPMC Univ Paris 06, LBM, 4 place Jussieu, 75005, Paris, France.|UMR 7203 LBM, CNRS, 75005, Paris, France.|Institut des Sciences et Ingénierie Chimiques, École polytechnique fédérale de Lausanne, 1015, Lausanne, Switzerland.
Geoffrey
G
Bodenhausen
École Normale Supérieure - PSL Research University, Département de Chimie, 24 rue Lhomond, 75005, Paris, France. fabien.ferrage@ens.fr.|Sorbonne Universités UPMC Univ Paris 06, LBM, 4 place Jussieu, 75005, Paris, France. fabien.ferrage@ens.fr.|UMR 7203 LBM, CNRS, 75005, Paris, France. fabien.ferrage@ens.fr.
Fabien
F
Ferrage
D050882:CREB-Binding Protein / Q000737:chemistry*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D054730:Protein Interaction Domains and Motifs; D025801:Ubiquitin / Q000737:chemistry*
D025801:Ubiquitin; D050882:CREB-Binding Protein; C494363:CREBBP protein, human
Adiabatic sweep; Cross-correlated cross relaxation; NMR; Protein dynamics