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. Journal of Biomolecular NMR, Dordrecht: Springer, 2015, vol. 63, No 4, p. 353-365. ISSN 0925-2738. doi:10.1007/s10858-015-9994-8.
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Basic information
Original name Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins
Authors KADEŘÁVEK, Pavel (203 Czechia, belonging to the institution), Sarina GRUTSCH (40 Austria), Nicola SALVI (756 Switzerland), Martin TOLLINGER (40 Austria), Lukáš ŽÍDEK (203 Czechia, guarantor, belonging to the institution), Geoffrey BODENHAUSEN (250 France) and Fabien FERRAGE (250 France).
Edition Journal of Biomolecular NMR, Dordrecht, Springer, 2015, 0925-2738.
Other information
Original language English
Type of outcome article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher Netherlands
Confidentiality degree is not subject to a state or trade secret
WWW Full Text
Impact factor Impact factor: 3.439
RIV identification code RIV/00216224:14740/15:00086418
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1007/s10858-015-9994-8
UT WoS 000365789500004
Keywords in English NMR; Protein dynamics; Adiabatic sweep; Cross-correlated cross relaxation
Tags OA, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Marie Šípková, DiS., učo 437722. Changed: 16. 12. 2019 14:22.
Abstract
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.
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12.251-Sciex-N-7, internal MU codeName: Motions in Disordered Proteins (Acronym: MoDiPro)
Investor: Foundation/Fund - foreign, Research and development projects
286154, internal MU codeName: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Acronym: SYLICA)
Investor: European Union, 7th Specific RTD Programme, Capacities
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