Details
| Original language | English |
|---|---|
| Article number | 100072 |
| Journal | Journal of Structural Biology: X |
| Volume | 6 |
| Early online date | 18 Aug 2022 |
| Publication status | Published - 2022 |
Abstract
Solid-state NMR (ssNMR) has become a well-established technique to study large and insoluble protein assemblies. However, its application to nucleic acid–protein complexes has remained scarce, mainly due to the challenges presented by overlapping nucleic acid signals. In the past decade, several efforts have led to the first structure determination of an RNA molecule by ssNMR. With the establishment of these tools, it has become possible to address the problem of structure determination of nucleic acid–protein complexes by ssNMR. Here we review first and more recent ssNMR methodologies that study nucleic acid–protein interfaces by means of chemical shift and peak intensity perturbations, direct distance measurements and paramagnetic effects. At the end, we review the first structure of an RNA–protein complex that has been determined from ssNMR-derived intermolecular restraints.
Keywords
- Intermolecular interfaces, Nucleic acid-protein complexes, ssNMR
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
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In: Journal of Structural Biology: X, Vol. 6, 100072, 2022.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Nucleic acid–protein interfaces studied by MAS solid-state NMR spectroscopy
AU - Aguion, Philipp Innig
AU - Marchanka, Alexander
AU - Carlomagno, Teresa
N1 - Funding Information: This work has received support from the DFG (Deutsche Forschungsgemeinschaft) grant CA294/21-1 to T.C.
PY - 2022
Y1 - 2022
N2 - Solid-state NMR (ssNMR) has become a well-established technique to study large and insoluble protein assemblies. However, its application to nucleic acid–protein complexes has remained scarce, mainly due to the challenges presented by overlapping nucleic acid signals. In the past decade, several efforts have led to the first structure determination of an RNA molecule by ssNMR. With the establishment of these tools, it has become possible to address the problem of structure determination of nucleic acid–protein complexes by ssNMR. Here we review first and more recent ssNMR methodologies that study nucleic acid–protein interfaces by means of chemical shift and peak intensity perturbations, direct distance measurements and paramagnetic effects. At the end, we review the first structure of an RNA–protein complex that has been determined from ssNMR-derived intermolecular restraints.
AB - Solid-state NMR (ssNMR) has become a well-established technique to study large and insoluble protein assemblies. However, its application to nucleic acid–protein complexes has remained scarce, mainly due to the challenges presented by overlapping nucleic acid signals. In the past decade, several efforts have led to the first structure determination of an RNA molecule by ssNMR. With the establishment of these tools, it has become possible to address the problem of structure determination of nucleic acid–protein complexes by ssNMR. Here we review first and more recent ssNMR methodologies that study nucleic acid–protein interfaces by means of chemical shift and peak intensity perturbations, direct distance measurements and paramagnetic effects. At the end, we review the first structure of an RNA–protein complex that has been determined from ssNMR-derived intermolecular restraints.
KW - Intermolecular interfaces
KW - Nucleic acid-protein complexes
KW - ssNMR
UR - http://www.scopus.com/inward/record.url?scp=85137123236&partnerID=8YFLogxK
U2 - 10.1016/j.yjsbx.2022.100072
DO - 10.1016/j.yjsbx.2022.100072
M3 - Article
AN - SCOPUS:85137123236
VL - 6
JO - Journal of Structural Biology: X
JF - Journal of Structural Biology: X
M1 - 100072
ER -