Details
| Original language | English |
|---|---|
| Title of host publication | Methods in Enzymology |
| Subtitle of host publication | Biological NMR Part B |
| Editors | A. Joshua Wand |
| Publisher | Academic Press Inc. |
| Chapter | 9 |
| Pages | 333-371 |
| Number of pages | 39 |
| Volume | 615 |
| ISBN (print) | 9780128167625 |
| Publication status | Published - 7 Dec 2018 |
Publication series
| Name | Methods in Enzymology |
|---|---|
| Volume | 615 |
| ISSN (Print) | 0076-6879 |
| ISSN (electronic) | 1557-7988 |
Abstract
RNA structure is essential to understand RNA function and regulation in cellular processes. RNA acts either in isolation or as part of a complex with proteins. Both isolated and protein-complexed RNA represent a challenge for structural biology, due to the complexity of its conformational space and intrinsic dynamics. NMR, with its capability to cope with dynamic structures, is the optimal technique to study RNA conformation, ideally in solution. However, RNA–protein complexes are often very large, which limits the application of solution-state NMR. In this chapter we describe the methodology that we developed to determine the structure of RNA by solid-state NMR. Solid-state NMR is not limited by large molecular weights and can be optimally applied to study both the RNA and the protein components of large RNA–protein complexes. We review the methods for resonance assignments, collection of RNA-specific distance restraints, as well as detection of protein–RNA interfaces.
Keywords
- Methodology, Protein–RNA complexes, Ribonucleic acids, RNA–protein complex, Solid-state NMR, Structure determination
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
Methods in Enzymology: Biological NMR Part B. ed. / A. Joshua Wand. Vol. 615 Academic Press Inc., 2018. p. 333-371 (Methods in Enzymology; Vol. 615).
Research output: Chapter in book/report/conference proceeding › Contribution to book/anthology › Research › peer review
}
TY - CHAP
T1 - Solid-State NMR Spectroscopy of RNA
AU - Marchanka, Alexander
AU - Carlomagno, Teresa
N1 - Publisher Copyright: © 2019 Elsevier Inc. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.
PY - 2018/12/7
Y1 - 2018/12/7
N2 - RNA structure is essential to understand RNA function and regulation in cellular processes. RNA acts either in isolation or as part of a complex with proteins. Both isolated and protein-complexed RNA represent a challenge for structural biology, due to the complexity of its conformational space and intrinsic dynamics. NMR, with its capability to cope with dynamic structures, is the optimal technique to study RNA conformation, ideally in solution. However, RNA–protein complexes are often very large, which limits the application of solution-state NMR. In this chapter we describe the methodology that we developed to determine the structure of RNA by solid-state NMR. Solid-state NMR is not limited by large molecular weights and can be optimally applied to study both the RNA and the protein components of large RNA–protein complexes. We review the methods for resonance assignments, collection of RNA-specific distance restraints, as well as detection of protein–RNA interfaces.
AB - RNA structure is essential to understand RNA function and regulation in cellular processes. RNA acts either in isolation or as part of a complex with proteins. Both isolated and protein-complexed RNA represent a challenge for structural biology, due to the complexity of its conformational space and intrinsic dynamics. NMR, with its capability to cope with dynamic structures, is the optimal technique to study RNA conformation, ideally in solution. However, RNA–protein complexes are often very large, which limits the application of solution-state NMR. In this chapter we describe the methodology that we developed to determine the structure of RNA by solid-state NMR. Solid-state NMR is not limited by large molecular weights and can be optimally applied to study both the RNA and the protein components of large RNA–protein complexes. We review the methods for resonance assignments, collection of RNA-specific distance restraints, as well as detection of protein–RNA interfaces.
KW - Methodology
KW - Protein–RNA complexes
KW - Ribonucleic acids
KW - RNA–protein complex
KW - Solid-state NMR
KW - Structure determination
UR - http://www.scopus.com/inward/record.url?scp=85057750844&partnerID=8YFLogxK
U2 - 10.1016/bs.mie.2018.08.029
DO - 10.1016/bs.mie.2018.08.029
M3 - Contribution to book/anthology
C2 - 30638533
AN - SCOPUS:85057750844
SN - 9780128167625
VL - 615
T3 - Methods in Enzymology
SP - 333
EP - 371
BT - Methods in Enzymology
A2 - Wand, A. Joshua
PB - Academic Press Inc.
ER -