Protein conformation by EPR spectroscopy using gadolinium tags clicked to genetically encoded p-azido-L-phenylalanine

Quantitative cysteine-independent ligation of a Gd(3+) tag to genetically encoded p-azido-L-phenylalanine via Cu(I)-catalyzed click chemistry is shown to deliver an exceptionally powerful tool for Gd(3+)-Gd(3+) distance measurements by double electron-electron resonance (DEER) experiments, as the po...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2015-01, Vol.51 (88), p.15898-15901
Hauptverfasser:	Abdelkader, E H, Feintuch, A, Yao, X, Adams, L A, Aurelio, L, Graham, B, Goldfarb, D, Otting, G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Azides - chemistry Carrier Proteins - chemical synthesis Carrier Proteins - chemistry Click Chemistry Deer Electron Spin Resonance Spectroscopy Escherichia coli - chemistry Gadolinium Glutamates - chemistry Mutagenesis, Site-Directed Phenylalanine - analogs & derivatives Phenylalanine - chemistry Phenylalanine - genetics Position measurement Protein Structure, Tertiary Proteins Spectroscopy Spin Labels Synthesis (chemistry) Tags
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Beschreibung
Zusammenfassung:	Quantitative cysteine-independent ligation of a Gd(3+) tag to genetically encoded p-azido-L-phenylalanine via Cu(I)-catalyzed click chemistry is shown to deliver an exceptionally powerful tool for Gd(3+)-Gd(3+) distance measurements by double electron-electron resonance (DEER) experiments, as the position of the Gd(3+) ion relative to the protein can be predicted with high accuracy.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/c5cc07121f