Ligand-driven conformational changes of MurD visualized by paramagnetic NMR

Proteins, especially multi-domain proteins, often undergo drastic conformational changes upon binding to ligands or by post-translational modifications, which is a key step to regulate their function. However, the detailed mechanisms of such dynamic regulation of the functional processes are poorly...

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Veröffentlicht in:	Scientific reports 2015-11, Vol.5 (1), p.16685-16685, Article 16685
Hauptverfasser:	Saio, Tomohide, Ogura, Kenji, Kumeta, Hiroyuki, Kobashigawa, Yoshihiro, Shimizu, Kazumi, Yokochi, Masashi, Kodama, Kota, Yamaguchi, Hiroto, Tsujishita, Hideki, Inagaki, Fuyuhiko
Format:	Artikel
Sprache:	eng
Schlagworte:	101/6 140/131 631/154/556 631/535/878/1263 82 Calorimetry Humanities and Social Sciences Ions Lanthanoid Series Elements - chemistry Ligands Magnetic Resonance Spectroscopy multidisciplinary Peptide Synthases - chemistry Protein Conformation Science
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