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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Published inChemical communications (Cambridge, England) Vol. 51; no. 88; pp. 15898 - 15901
Main Authors Abdelkader, E H, Feintuch, A, Yao, X, Adams, L A, Aurelio, L, Graham, B, Goldfarb, D, Otting, G
Format Journal Article
LanguageEnglish
Published England 01.01.2015
Subjects
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)
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1359-7345
1364-548X
DOI:10.1039/c5cc07121f