F7376
4-Fluoro-DL-tryptophan
crystalline
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About This Item
Fórmula empírica (notación de Hill):
C11H11FN2O2
Número de CAS:
Peso molecular:
222.22
Número MDL:
Código UNSPSC:
12352200
ID de la sustancia en PubChem:
NACRES:
NA.26
Productos recomendados
Ensayo
≥98.0% (TLC)
Formulario
crystalline
técnicas
NMR: suitable
color
off-white
temp. de almacenamiento
−20°C
cadena SMILES
NC(Cc1c[nH]c2cccc(F)c12)C(O)=O
InChI
1S/C11H11FN2O2/c12-7-2-1-3-9-10(7)6(5-14-9)4-8(13)11(15)16/h1-3,5,8,14H,4,13H2,(H,15,16)
Clave InChI
DEBQMEYEKKWIKC-UHFFFAOYSA-N
Acciones bioquímicas o fisiológicas
4-Fluoro-DL-tryptophan (4-F-TRP) is used to label bacterial arginyl-tRNA synthetases for conformational analysis and to label myoglobins and hemoglobins for NMR spectra analysis.
Código de clase de almacenamiento
13 - Non Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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P Soumillion et al.
Biochemistry, 37(7), 1819-1827 (1998-03-04)
Clamp proteins confer processivity to the DNA polymerase during DNA replication. These oligomeric proteins are loaded onto DNA by clamp loader protein complexes in an ATP-dependent manner. The mechanism by which the trimeric bacteriophage T4 clamp protein (the 45 protein)
J L Hott et al.
The Biochemical journal, 264(1), 297-299 (1989-11-15)
The derivative 4-fluorotryptophan was confirmed to have negligible fluorescence at 25 degrees C and 285 nm (tryptophan/4-fluorotryptophan quantum-yield ratio greater than 100:1). However, photolysis experiments on tryptophan and 4-fluorotryptophan, in which loss of starting material was measured by reverse-phase h.p.l.c.
J G Pearson et al.
Biochemistry, 36(12), 3590-3599 (1997-03-25)
We have obtained the 470 MHz 19F NMR spectra of wild type [4-F]Trp-labeled myoglobins (MbCO, MbO2, deoxyMb, metMb, and MbCN) and hemoglobins (HbCO, HbO2, and deoxyHb), as well as those of several mutants (W7F Mb, betaW15F Hb, betaW37S Hb, and
J T Wong
Proceedings of the National Academy of Sciences of the United States of America, 80(20), 6303-6306 (1983-10-01)
Bacillus subtilis strain QB928, a tryptophan-auxotroph, was serially mutated to yield strain HR15. For QB928, tryptophan functioned as a competent amino acid and 4-fluorotryptophan as merely an inferior analogue. For HR15, these roles were reversed. The tryptophan/4-fluorotryptophan growth ratio decreased
P M Bronskill et al.
The Biochemical journal, 249(1), 305-308 (1988-01-01)
The tryptophan-auxotrophic Bacillus subtilis LC33 mutant strain utilizes either tryptophan or 4-fluorotryptophan for growth. Proteins therefore could be isolated from these cells in either tryptophan-containing or 4-fluorotryptophan-containing forms. Since 4-fluorotryptophan is non-fluorescent, tryptophan fluorescence would be suppressed in the 4-fluorotryptophan-containing
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