ArticleJournal of biomolecular NMR2015
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA).
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Sparse pseudocontact shift NMR data obtained from a non-canonical amino acid-linked lanthanide tag improves integral membrane protein structure prediction.Journal of biomolecular NMR · 2023Article
- A Chemical Biology Primer for NMR Spectroscopists.Journal of magnetic resonance open · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- NMR Methods for Structural Characterization of Protein-Protein Complexes.Frontiers in molecular biosciences · 2020Article
- A Double-Armed, Hydrophilic Transition Metal Complex as a Paramagnetic NMR Probe.Angewandte Chemie (International ed. in English) · 2019Review
- Probing Protein-Protein Interactions Using Asymmetric Labeling and Carbonyl-Carbon Selective Heteronuclear NMR Spectroscopy.Molecules (Basel, Switzerland) · 2018Review
- Interaction of Monomeric Interleukin-8 with CXCR1 Mapped by Proton-Detected Fast MAS Solid-State NMR.Biophysical journal · 2017Article
- Structure of monomeric Interleukin-8 and its interactions with the N-terminal Binding Site-I of CXCR1 by solution NMR spectroscopy.Journal of biomolecular NMR · 2017Article
- Lanthanoid tagging via an unnatural amino acid for protein structure characterization.Journal of biomolecular NMR · 2017Article
- A molecular engineering toolbox for the structural biologist.Quarterly reviews of biophysics · 2017Review
- At the Interface of Chemical and Biological Synthesis: An Expanded Genetic Code.Cold Spring Harbor perspectives in biology · 2016Review
- Site-specific tagging proteins with a rigid, small and stable transition metal chelator, 8-hydroxyquinoline, for paramagnetic NMR analysis.Journal of biomolecular NMR · 2016Article
- An encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteins.Journal of biomolecular NMR · 2016Article
- Structure determination of uniformly (13)C, (15)N labeled protein using qualitative distance restraints from MAS solid-state (13)C-NMR observed paramagnetic relaxation enhancement.Journal of biomolecular NMR · 2016Article
- NMR studies of membrane proteins.Journal of biomolecular NMR · 2015Article
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6 authors at 1 institution in 1 country.
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Abstract
The use of paramagnetic constraints in protein NMR is an active area of research because of the benefits of long-range distance measurements (>10 Å). One of the main issues in successful execution is the incorporation of a paramagnetic metal ion into diamagnetic proteins. The most common metal ion tags are relatively long aliphatic chains attached to the side chain of a selected cysteine residue with a chelating group at the end where it can undergo substantial internal motions, decreasing the accuracy of the method. An attractive alternative approach is to incorporate an unnatural amino acid that binds metal ions at a specific site on the protein using the methods of molecular biology. Here we describe the successful incorporation of the unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA) into two different membrane proteins by heterologous expression in E. coli. Fluorescence and NMR experiments demonstrate complete replacement of the natural amino acid with HQA and stable metal chelation by the mutated proteins. Evidence of site-specific intra- and inter-molecular PREs by NMR in micelle solutions sets the stage for the use of HQA incorporation in solid-state NMR structure determinations of membrane proteins in phospholipid bilayers.
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