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Journal Abstract Search

264 related items for PubMed ID: 28856561

  • 1. Site-selective 13C labeling of histidine and tryptophan using ribose.
    Weininger U.
    J Biomol NMR; 2017 Sep; 69(1):23-30. PubMed ID: 28856561
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  • 2. Site-selective 13C labeling of proteins using erythrose.
    Weininger U.
    J Biomol NMR; 2017 Mar; 67(3):191-200. PubMed ID: 28247186
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  • 3. Conformational exchange of aromatic side chains by 1H CPMG relaxation dispersion.
    Raum HN, Dreydoppel M, Weininger U.
    J Biomol NMR; 2018 Oct; 72(1-2):105-114. PubMed ID: 30229369
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  • 4. Use of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
    Rodriguez-Mias RA, Pellecchia M.
    J Am Chem Soc; 2003 Mar 12; 125(10):2892-3. PubMed ID: 12617653
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  • 5. Chemo-enzymatic synthesis of selectively ¹³C/¹⁵N-labeled RNA for NMR structural and dynamics studies.
    Alvarado LJ, Longhini AP, LeBlanc RM, Chen B, Kreutz C, Dayie TK.
    Methods Enzymol; 2014 Mar 12; 549():133-62. PubMed ID: 25432748
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  • 6. Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues.
    Löhr F, Rogov VV, Shi M, Bernhard F, Dötsch V.
    J Biomol NMR; 2005 Aug 12; 32(4):309-28. PubMed ID: 16211484
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  • 7. Alternate-site isotopic labeling of ribonucleotides for NMR studies of ribose conformational dynamics in RNA.
    Johnson JE, Julien KR, Hoogstraten CG.
    J Biomol NMR; 2006 Aug 12; 35(4):261-74. PubMed ID: 16937241
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  • 12. Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy.
    Lacabanne D, Meier BH, Böckmann A.
    J Biomol NMR; 2018 Jul 12; 71(3):141-150. PubMed ID: 29197975
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  • 14. Highly Selective Stable Isotope Labeling of Histidine Residues by Using a Novel Precursor in E. coli-Based Overexpression Systems.
    Schörghuber J, Geist L, Platzer G, Konrat R, Lichtenecker RJ.
    Chembiochem; 2017 Aug 04; 18(15):1487-1491. PubMed ID: 28489326
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  • 17. Amino Acid Selective 13C Labeling and 13C Scrambling Profile Analysis of Protein α and Side-Chain Carbons in Escherichia coli Utilized for Protein Nuclear Magnetic Resonance.
    Sugiki T, Furuita K, Fujiwara T, Kojima C.
    Biochemistry; 2018 Jul 03; 57(26):3576-3589. PubMed ID: 29924600
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