-
Je něco špatně v tomto záznamu ?
MAS dependent sensitivity of different isotopomers in selectively methyl protonated protein samples in solid state NMR
K. Xue, R. Sarkar, Z. Tosner, D. Lalli, C. Motz, B. Koch, G. Pintacuda, B. Reif,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články
Grantová podpora
ERC-2014-CoG "P-MEM-NMR" GA n 648974
European Research Council - International
GA 653706
EU access project iNext
Project B07
Deutsche Forschungsgemeinschaft
SFB-1035
Deutsche Forschungsgemeinschaft
Grant Re1435
Deutsche Forschungsgemeinschaft
NLK
ProQuest Central
od 1997-01-01 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2000-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 1997-01-01 do Před 1 rokem
- MeSH
- deuterium chemie MeSH
- metylace * MeSH
- nukleární magnetická rezonance biomolekulární metody MeSH
- protony * MeSH
- senzitivita a specificita MeSH
- spektrin chemie MeSH
- src homologní domény MeSH
- Publikační typ
- časopisecké články MeSH
Sensitivity and resolution together determine the quality of NMR spectra in biological solids. For high-resolution structure determination with solid-state NMR, proton-detection emerged as an attractive strategy in the last few years. Recent progress in probe technology has extended the range of available MAS frequencies up to above 100 kHz, enabling the detection of resolved resonances from sidechain protons, which are important reporters of structure. Here we characterise the interplay between MAS frequency in the newly available range of 70-110 kHz and proton content on the spectral quality obtainable on a 1 GHz spectrometer for methyl resonances. Variable degrees of proton densities are tested on microcrystalline samples of the α-spectrin SH3 domain with selectively protonated methyl isotopomers (CH3, CH2D, CHD2) in a perdeuterated matrix. The experimental results are supported by simulations that allow the prediction of the sensitivity outside this experimental frequency window. Our results facilitate the selection of the appropriate labelling scheme at a given MAS rotation frequency.
Helmholtz Zentrum München Lichtenbergstr 4 85747 Garching Germany
Munich Center for Integrated Protein Science Lichtenbergstr 4 85747 Garching Germany
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc20023529
- 003
- CZ-PrNML
- 005
- 20201214130310.0
- 007
- ta
- 008
- 201125s2019 ne f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1007/s10858-019-00274-0 $2 doi
- 035 __
- $a (PubMed)31515660
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a ne
- 100 1_
- $a Xue, Kai $u Helmholtz-Zentrum München (HMGU), Deutsches Forschungszentrum für Gesundheit und Umwelt, Ingolstädter Landstr. 1, 85764, Neuherberg, Germany.
- 245 10
- $a MAS dependent sensitivity of different isotopomers in selectively methyl protonated protein samples in solid state NMR / $c K. Xue, R. Sarkar, Z. Tosner, D. Lalli, C. Motz, B. Koch, G. Pintacuda, B. Reif,
- 520 9_
- $a Sensitivity and resolution together determine the quality of NMR spectra in biological solids. For high-resolution structure determination with solid-state NMR, proton-detection emerged as an attractive strategy in the last few years. Recent progress in probe technology has extended the range of available MAS frequencies up to above 100 kHz, enabling the detection of resolved resonances from sidechain protons, which are important reporters of structure. Here we characterise the interplay between MAS frequency in the newly available range of 70-110 kHz and proton content on the spectral quality obtainable on a 1 GHz spectrometer for methyl resonances. Variable degrees of proton densities are tested on microcrystalline samples of the α-spectrin SH3 domain with selectively protonated methyl isotopomers (CH3, CH2D, CHD2) in a perdeuterated matrix. The experimental results are supported by simulations that allow the prediction of the sensitivity outside this experimental frequency window. Our results facilitate the selection of the appropriate labelling scheme at a given MAS rotation frequency.
- 650 _2
- $a deuterium $x chemie $7 D003903
- 650 12
- $a metylace $7 D008745
- 650 _2
- $a nukleární magnetická rezonance biomolekulární $x metody $7 D019906
- 650 12
- $a protony $7 D011522
- 650 _2
- $a senzitivita a specificita $7 D012680
- 650 _2
- $a spektrin $x chemie $7 D013049
- 650 _2
- $a src homologní domény $7 D018909
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Sarkar, Riddhiman $u Helmholtz-Zentrum München (HMGU), Deutsches Forschungszentrum für Gesundheit und Umwelt, Ingolstädter Landstr. 1, 85764, Neuherberg, Germany. riddhiman.sarkar@helmholtz-muenchen.de. Munich Center for Integrated Protein Science (CIPS-M) at Department Chemie, Technische Universität München (TUM), Lichtenbergstr. 4, 85747, Garching, Germany. riddhiman.sarkar@helmholtz-muenchen.de.
- 700 1_
- $a Tosner, Zdenek $u Department of Chemistry, Faculty of Science, Charles University, Hlavova 8, 12842, Prague 2, Czech Republic.
- 700 1_
- $a Lalli, Daniela $u Centre de Résonance Magnétique Nucléaire a Très hauts Champs (FRE 2034, CNRS, Ecole Normale Supérieure de Lyon, Université Claude Bernard Lyon 1), Université de Lyon, 5 Rue de la Doua, 69100, Villeurbanne, France.
- 700 1_
- $a Motz, Carina $u Munich Center for Integrated Protein Science (CIPS-M) at Department Chemie, Technische Universität München (TUM), Lichtenbergstr. 4, 85747, Garching, Germany.
- 700 1_
- $a Koch, Benita $u Munich Center for Integrated Protein Science (CIPS-M) at Department Chemie, Technische Universität München (TUM), Lichtenbergstr. 4, 85747, Garching, Germany.
- 700 1_
- $a Pintacuda, Guido $u Centre de Résonance Magnétique Nucléaire a Très hauts Champs (FRE 2034, CNRS, Ecole Normale Supérieure de Lyon, Université Claude Bernard Lyon 1), Université de Lyon, 5 Rue de la Doua, 69100, Villeurbanne, France. Dipartimento di Scienze e Innovazione Tecnologica, Università del Piemonte Orientale Amedeo Avogadro, Viale Teresa Michel, 15121, Alessandria, Italy.
- 700 1_
- $a Reif, Bernd $u Helmholtz-Zentrum München (HMGU), Deutsches Forschungszentrum für Gesundheit und Umwelt, Ingolstädter Landstr. 1, 85764, Neuherberg, Germany. reif@tum.de. Munich Center for Integrated Protein Science (CIPS-M) at Department Chemie, Technische Universität München (TUM), Lichtenbergstr. 4, 85747, Garching, Germany. reif@tum.de.
- 773 0_
- $w MED00005454 $t Journal of biomolecular NMR $x 1573-5001 $g Roč. 73, č. 10-11 (2019), s. 625-631
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/31515660 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20201125 $b ABA008
- 991 __
- $a 20201214130309 $b ABA008
- 999 __
- $a ok $b bmc $g 1595848 $s 1114205
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2019 $b 73 $c 10-11 $d 625-631 $e 20190912 $i 1573-5001 $m Journal of biomolecular NMR $n J Biomol NMR $x MED00005454
- GRA __
- $a ERC-2014-CoG "P-MEM-NMR" GA n 648974 $p European Research Council $2 International
- GRA __
- $a GA 653706 $p EU access project iNext
- GRA __
- $a Project B07 $p Deutsche Forschungsgemeinschaft
- GRA __
- $a SFB-1035 $p Deutsche Forschungsgemeinschaft
- GRA __
- $a Grant Re1435 $p Deutsche Forschungsgemeinschaft
- LZP __
- $a Pubmed-20201125