Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins

Logo poskytovatele

Varování

Publikace nespadá pod Pedagogickou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
Autoři

KADEŘÁVEK Pavel GRUTSCH Sarina SALVI Nicola TOLLINGER Martin ŽÍDEK Lukáš BODENHAUSEN Geoffrey FERRAGE Fabien

Rok publikování 2015
Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Biomolecular NMR
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www Full Text
Doi http://dx.doi.org/10.1007/s10858-015-9994-8
Obor Biochemie
Klíčová slova NMR; Protein dynamics; Adiabatic sweep; Cross-correlated cross relaxation
Přiložené soubory
Popis 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.
Související projekty:

Používáte starou verzi internetového prohlížeče. Doporučujeme aktualizovat Váš prohlížeč na nejnovější verzi.