Details
| Original language | English |
|---|---|
| Title of host publication | Methods in Molecular Biology |
| Pages | 3-23 |
| Number of pages | 21 |
| ISBN (electronic) | 978-1-0716-3393-9 |
| Publication status | Published - 6 Sept 2023 |
Publication series
| Name | Methods in Molecular Biology |
|---|---|
| Volume | 2705 |
| ISSN (Print) | 1064-3745 |
| ISSN (electronic) | 1940-6029 |
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique to solve the structure of biomolecular complexes at atomic resolution in solution. Small proteins such as Src-homology 2 (SH2) domains have fast tumbling rates and long-lived NMR signals, making them particularly suited to be studied by standard NMR methods. SH2 domains are modular proteins whose function is the recognition of sequences containing phosphotyrosines. In this chapter, we describe the application of NMR to assess the interaction between SH2 domains and phosphopeptides and determine the structure of the resulting complexes.
Keywords
- Intermolecular interactions, Nuclear magnetic resonance (NMR) spectroscopy, Phosphopeptides, Phosphotyrosine, Src-homology 2 (SH2) domain, Structure determination
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
Cite this
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Methods in Molecular Biology. 2023. p. 3-23 (Methods in Molecular Biology; Vol. 2705).
Research output: Chapter in book/report/conference proceeding › Contribution to book/anthology › Research › peer review
}
TY - CHAP
T1 - Methods for Structure Determination of SH2 Domain–Phosphopeptide Complexes by NMR
AU - Nanna, Vittoria
AU - Marasco, Michelangelo
AU - Kirkpatrick, John P.
AU - Carlomagno, Teresa
N1 - Publisher Copyright: © The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature 2023.
PY - 2023/9/6
Y1 - 2023/9/6
N2 - Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique to solve the structure of biomolecular complexes at atomic resolution in solution. Small proteins such as Src-homology 2 (SH2) domains have fast tumbling rates and long-lived NMR signals, making them particularly suited to be studied by standard NMR methods. SH2 domains are modular proteins whose function is the recognition of sequences containing phosphotyrosines. In this chapter, we describe the application of NMR to assess the interaction between SH2 domains and phosphopeptides and determine the structure of the resulting complexes.
AB - Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique to solve the structure of biomolecular complexes at atomic resolution in solution. Small proteins such as Src-homology 2 (SH2) domains have fast tumbling rates and long-lived NMR signals, making them particularly suited to be studied by standard NMR methods. SH2 domains are modular proteins whose function is the recognition of sequences containing phosphotyrosines. In this chapter, we describe the application of NMR to assess the interaction between SH2 domains and phosphopeptides and determine the structure of the resulting complexes.
KW - Intermolecular interactions
KW - Nuclear magnetic resonance (NMR) spectroscopy
KW - Phosphopeptides
KW - Phosphotyrosine
KW - Src-homology 2 (SH2) domain
KW - Structure determination
UR - http://www.scopus.com/inward/record.url?scp=85169847008&partnerID=8YFLogxK
U2 - 10.1007/978-1-0716-3393-9_1
DO - 10.1007/978-1-0716-3393-9_1
M3 - Contribution to book/anthology
C2 - 37668966
AN - SCOPUS:85169847008
SN - 978-1-0716-3392-2
T3 - Methods in Molecular Biology
SP - 3
EP - 23
BT - Methods in Molecular Biology
ER -