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Titolo:
Elucidation of solvent exposure, side-chain reactivity, and steric demandsof the trifluoromethionine residue in a recombinant protein
Autore:
Duewel, HS; Daub, E; Robinson, V; Honek, JF;
Indirizzi:
Univ Waterloo, Dept Chem, Waterloo, ON N2L 3G1, Canada Univ Waterloo Waterloo ON Canada N2L 3G1 em, Waterloo, ON N2L 3G1, Canada Univ Guelph, Dept Chem & Biochem, Guelph, ON N1G 2W1, Canada Univ Guelph Guelph ON Canada N1G 2W1 Biochem, Guelph, ON N1G 2W1, Canada
Titolo Testata:
BIOCHEMISTRY
fascicolo: 44, volume: 40, anno: 2001,
pagine: 13167 - 13176
SICI:
0006-2960(20011106)40:44<13167:EOSESR>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-LACTATE DEHYDROGENASE; NMR CHEMICAL-SHIFTS; F-19 NMR; MAGNETIC-RESONANCE; ESCHERICHIA-COLI; GLUTATHIONE TRANSFERASE; CONFORMATIONAL-CHANGES; BACTERIOPHAGE-LAMBDA; DIHYDROFOLATE-REDUCTASE; CRYSTAL-STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Honek, JF Univ Waterloo, Dept Chem, 200 Univ Ave, Waterloo, ON N2L 3G1, Canada Univ Waterloo 200 Univ Ave Waterloo ON Canada N2L 3G1 G1, Canada
Citazione:
H.S. Duewel et al., "Elucidation of solvent exposure, side-chain reactivity, and steric demandsof the trifluoromethionine residue in a recombinant protein", BIOCHEM, 40(44), 2001, pp. 13167-13176

Abstract

When incorporated into proteins, fluorinated amino acids have been utilized as F-19 NMR probes of protein structure and protein-ligand interactions, and as subtle structural replacements for their parent amino acids which isnot 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 bioincorporatedinto recombinant proteins and to be extremely useful as F-19 NMR biophysical probes. Interestingly, in the case of the bacteriophage lambda lysozyme (LaL) which contains only three Met residues (at positions 1, 14, and 107),four F-19 NMR resonances are observed when TFM is incorporated into LaL. To elucidate the underlying structural reasons for this anomalous observation and to more fully explore the effect of TFM on protein structure, site-directed mutagenesis was used to assign each F-19 NMR resonance. Incorporation of TFM into the M14L mutant resulted in the collapse of the two F-19 resonances associated with TFM at position 107 into a single resonance, suggesting that when position 14 in wild-type protein contains TFM, a subtle but different environment exists for the methionine at position 107. In addition, F-19 and [H-1-C-13]-HMQC NMR experiments have been utilized with paramagnetic line broadening and K2PtCl4 reactivity experiments to obtain information about the probable spatial position of each Met in the protein. These results are compared with the recently determined crystal structure of LaL and allow for a more detailed structural explanation for the effect of fluorination on protein structure.

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Documento generato il 03/12/20 alle ore 15:11:33