2001
DOI: 10.1021/bi011381b
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Elucidation of Solvent Exposure, Side-Chain Reactivity, and Steric Demands of the Trifluoromethionine Residue in a Recombinant Protein

Abstract: When incorporated into proteins, fluorinated amino acids have been utilized as 19F NMR probes of protein structure and protein-ligand interactions, and as subtle structural replacements for their parent amino acids which is not possible using the standard 20-amino acid repertoire. Recent investigations have shown the ability of various fluorinated methionines, such as difluoromethionine (DFM) and trifluoromethionine (TFM), to be bioincorporated into recombinant proteins and to be extremely useful as 19F NMR bi… Show more

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Cited by 47 publications
(36 citation statements)
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“…Likewise, when incorporated into bacteriophage l lysozyme, difluoromethionine, 4, which is diastereotopic in nature, exhibited a significant difference in the chemical shifts observed between the surface-exposed methionine residues and those found in the tightly packed core of the enzyme [27]. Similarly, trifluoromethionine, 5, was incorporated into phage lysozyme to probe the functions of methionine residues in the protein, and has also been used as a unique probe to study protein-ligand interactions [28]. Incorporation of 4 into the crucial methionine-turn region of alkaline protease was used to investigate the role of methionine in the structural and catalytic properties of the protein [29].…”
Section: Biophysical Probesmentioning
confidence: 99%
“…Likewise, when incorporated into bacteriophage l lysozyme, difluoromethionine, 4, which is diastereotopic in nature, exhibited a significant difference in the chemical shifts observed between the surface-exposed methionine residues and those found in the tightly packed core of the enzyme [27]. Similarly, trifluoromethionine, 5, was incorporated into phage lysozyme to probe the functions of methionine residues in the protein, and has also been used as a unique probe to study protein-ligand interactions [28]. Incorporation of 4 into the crucial methionine-turn region of alkaline protease was used to investigate the role of methionine in the structural and catalytic properties of the protein [29].…”
Section: Biophysical Probesmentioning
confidence: 99%
“…[225] Fluorine-substituted amino acids can be used as NMR probes. For example, fluoromethionine has been substituted for methionine in bacteriophage l-lysozyme to study ligand binding by 19 F NMR spectroscopy, [226][227][228] and fluorinated tryptophan has been incorporated for 19 F NMR studies in cyan fluorescent protein [229] and the chaperone PapD. [230] Nonproteinogenic functional groups that provide selective handles for further protein modification have also been introduced into proteins by these methods.…”
Section: Applicationsmentioning
confidence: 99%
“…By using RSI, selenomethionine [120], difluoromethionine [125], trifluoromethionine [126], norleucine [123,127], homopropargylglycine (Hpg) [128], azidohomoalanine (Aha) [129], homoallylglycine (Hag) [130], and methoxinine [127] have been incorporated using methionyl-tRNA synthetase (MetRS); per-thiaproline, 3 [131,132]; trifluorovaline (TfV), 2-amino-3-methyl-4-pentenoic acid have been incorporated using isoleucyl-tRNA synthetase (IleRS) [133][134][135]; o-fluorophenylalanine, m-fluorophenylalanine, pFF [136], 2-pyridylalanine, 3-pyridylalanine, and 4-pyridylalanine [137] have been incorporated using PheRS; 4-aminotryptophan (4AW), 5-aminotryptophan (5AW), 4-fluorotryptophan (4FW), 6-fluorotryptophan (6FW), 5-hydroxytryptophan (5HW), 7AzW have been incorporated using TyrRS [138][139][140][141]; and trifluoroleucine has been incorporated using leucyl-tRNA synthetase (LeuRS) [142,143] in E. coli (Table 12.3). Budisa and coworkers have explored RSI for the integration of Hpg and norleucine into the superoxide dismutase (SOD) protein in yeast [123].…”
Section: Endogenous Aarsmentioning
confidence: 99%