ArticleProtein science : a publication of the Protein Society2011
Site-specific ¹⁹F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 34 citations in OpenAlex.
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- Protein-protein interaction analysis in crude bacterial lysates using combinational method ofProtein & cell · 2017Article
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- Nano-size uni-lamellar lipodisq improved in situ auto-phosphorylation analysis of E. coli tyrosine kinase using (19)F nuclear magnetic resonance.Protein & cell · 2015Article
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- Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs.Current opinion in structural biology · 2013Review
- Advances in NMR structures of integral membrane proteins.Current opinion in structural biology · 2013Review
- The quiet renaissance of protein nuclear magnetic resonance.Biochemistry · 2013Review
- Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutant.ACS chemical biology · 2013Article
- Alternative pathways of human islet amyloid polypeptide aggregation distinguished by (19)f nuclear magnetic resonance-detected kinetics of monomer consumption.Biochemistry · 2012Article
- In situ 19F NMR studies of an E. coli membrane protein.Protein science : a publication of the Protein Society · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site-specific ¹⁹F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, one-dimensional ¹⁹F spectra and T₁, T₂ relaxation data were acquired on a SH3 domain in aqueous buffer containing 60% glycerol, and a nine-transmembrane helices membrane protein diacyl-glycerol kinase (DAGK) in dodecyl phosphochoine (DPC) micelles. The high quality of the data indicates that this method can be applied to site-specifically analyze side chain internal mobility of membrane proteins or large size proteins.
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