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

J 2015

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

KADEŘÁVEK, Pavel, Sarina GRUTSCH, Nicola SALVI, Martin TOLLINGER, Lukáš ŽÍDEK et. al.

Základní údaje

Originální název

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

Autoři

KADEŘÁVEK, Pavel (203 Česká republika, domácí), Sarina GRUTSCH (40 Rakousko), Nicola SALVI (756 Švýcarsko), Martin TOLLINGER (40 Rakousko), Lukáš ŽÍDEK (203 Česká republika, garant, domácí), Geoffrey BODENHAUSEN (250 Francie) a Fabien FERRAGE (250 Francie)

Vydání

Journal of Biomolecular NMR, Dordrecht, Springer, 2015, 0925-2738

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Full Text

Impakt faktor

Impact factor: 3.439

Kód RIV

RIV/00216224:14740/15:00086418

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1007/s10858-015-9994-8

UT WoS

000365789500004

Klíčová slova anglicky

NMR; Protein dynamics; Adiabatic sweep; Cross-correlated cross relaxation

Štítky

OA, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 16. 12. 2019 14:22, Mgr. Marie Šípková, DiS.

Anotace

V originále

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.

Návaznosti

12.251-Sciex-N-7, interní kód MU

Název: Motions in Disordered Proteins (Akronym: MoDiPro)

Investor: Ostatní - zahraniční, Motions in Disordered Proteins

286154, interní kód MU

Název: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Akronym: SYLICA)

Investor: Evropská unie, SYLICA - Synergies of Life and Material Sciences to Create a New Future, Kapacity

Přiložené soubory

1333976_Cross-correlated.pdf

Požádat o autorskou verzi souboru

Citovat

KADEŘÁVEK, Pavel, Sarina GRUTSCH, Nicola SALVI, Martin TOLLINGER, Lukáš ŽÍDEK, Geoffrey BODENHAUSEN a Fabien FERRAGE. Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins. Journal of Biomolecular NMR. Dordrecht: Springer, 2015, roč. 63, č. 4, s. 353-365. ISSN 0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-015-9994-8.

@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 a Fabien FERRAGE. Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins. \textit{Journal of Biomolecular NMR}. Dordrecht: Springer, 2015, roč.~63, č.~4, s.~353-365. ISSN~0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-015-9994-8.

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