+検索条件
-Structure paper
タイトル | Cryo-EM and solid state NMR together provide a more comprehensive structural investigation of protein fibrils. |
---|---|
ジャーナル・号・ページ | Protein Sci, Vol. 33, Issue 10, Page e5168, Year 2024 |
掲載日 | 2024年9月14日 |
著者 | Blake D Fonda / Masato Kato / Yang Li / Dylan T Murray / |
PubMed 要旨 | The tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study ...The tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study demonstrates the complementary nature of these two structural biology techniques. Chemical shift assignments from solid state NMR are used to determine the secondary structure at the level of individual amino acids, which is faithfully seen in cryo-EM reconstructions. Additionally, solid state NMR demonstrates that the region not observed in the reconstructed cryo-EM density is primarily in a highly mobile random coil conformation rather than adopting multiple rigid conformations. Overall, this study illustrates the benefit of investigations combining cryo-EM and solid state NMR to investigate protein fibril structure. |
リンク | Protein Sci / PubMed:39276003 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.31 Å |
構造データ | EMDB-45130, PDB-9c1u: |
由来 |
|
キーワード | PROTEIN FIBRIL |