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@article{1333976, author = {Kadeřávek, Pavel and Grutsch, Sarina and Salvi, Nicola and Tollinger, Martin and Žídek, Lukáš and Bodenhausen, Geoffrey and Ferrage, Fabien}, article_location = {Dordrecht}, article_number = {4}, doi = {http://dx.doi.org/10.1007/s10858-015-9994-8}, keywords = {NMR; Protein dynamics; Adiabatic sweep; Cross-correlated cross relaxation}, language = {eng}, issn = {0925-2738}, journal = {Journal of Biomolecular NMR}, title = {Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins}, url = {http://download.springer.com/static/pdf/7/art%253A10.1007%252Fs10858-015-9994-8.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs10858-015-9994-8&token2=exp=1454485862~acl=%2Fstatic%2Fpdf%2F7%2Fart%25253A10.1007%25252Fs10858-015-9994-8}, volume = {63}, year = {2015} }
TY - JOUR ID - 1333976 AU - Kadeřávek, Pavel - Grutsch, Sarina - Salvi, Nicola - Tollinger, Martin - Žídek, Lukáš - Bodenhausen, Geoffrey - Ferrage, Fabien PY - 2015 TI - Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins JF - Journal of Biomolecular NMR VL - 63 IS - 4 SP - 353-365 EP - 353-365 PB - Springer SN - 09252738 KW - NMR KW - Protein dynamics KW - Adiabatic sweep KW - Cross-correlated cross relaxation UR - http://download.springer.com/static/pdf/7/art%253A10.1007%252Fs10858-015-9994-8.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs10858-015-9994-8&token2=exp=1454485862~acl=%2Fstatic%2Fpdf%2F7%2Fart%25253A10.1007%25252Fs10858-015-9994-8 L2 - http://download.springer.com/static/pdf/7/art%253A10.1007%252Fs10858-015-9994-8.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs10858-015-9994-8&token2=exp=1454485862~acl=%2Fstatic%2Fpdf%2F7%2Fart%25253A10.1007%25252Fs10858-015-9994-8 N2 - 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 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. ER -
KADEŘÁVEK, Pavel, Sarina GRUTSCH, Nicola SALVI, Martin TOLLINGER, Lukáš ŽÍDEK, Geoffrey BODENHAUSEN and Fabien FERRAGE. Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer, 2015, vol.~63, No~4, p.~353-365. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-015-9994-8.
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