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
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Abstract 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.
AbstractList Quantitative cysteine-independent ligation of a Gd super(3+) tag to genetically encoded p-azido-l-phenylalanine viaCu(i)-catalyzed click chemistry is shown to deliver an exceptionally powerful tool for Gd super(3+)-Gd super(3+) distance measurements by double electron-electron resonance (DEER) experiments, as the position of the Gd super(3+) ion relative to the protein can be predicted with high accuracy.
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.
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.
Author Aurelio, L
Feintuch, A
Otting, G
Abdelkader, E H
Yao, X
Adams, L A
Goldfarb, D
Graham, B
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/26391199$$D View this record in MEDLINE/PubMed
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Snippet 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...
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...
Quantitative cysteine-independent ligation of a Gd super(3+) tag to genetically encoded p-azido-l-phenylalanine viaCu(i)-catalyzed click chemistry is shown to...
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pubmed
SourceType Aggregation Database
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StartPage 15898
SubjectTerms 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
Title Protein conformation by EPR spectroscopy using gadolinium tags clicked to genetically encoded p-azido-L-phenylalanine
URI https://www.ncbi.nlm.nih.gov/pubmed/26391199
https://search.proquest.com/docview/1728054717
https://search.proquest.com/docview/1768585312
https://search.proquest.com/docview/1770284739
Volume 51
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link.rule.ids 315,783,787,27936,27937
linkProvider Royal Society of Chemistry
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