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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00086418" target="_blank" >RIV/00216224:14740/15:00086418 - isvavai.cz</a>

Výsledek na webu

<a href="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" target="_blank" >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</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s10858-015-9994-8" target="_blank" >10.1007/s10858-015-9994-8</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Biomolecular NMR

ISSN

0925-2738

e-ISSN

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Svazek periodika

63

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

13

Strana od-do

353-365

Kód UT WoS článku

000365789500004

EID výsledku v databázi Scopus

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