F7376
4-Fluoro-DL-tryptophan
crystalline
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关于此项目
经验公式（希尔记法）:
C11H11FN2O2
化学文摘社编号:
分子量:
222.22
NACRES:
NA.26
PubChem Substance ID:
UNSPSC Code:
12352200
MDL number:
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)
SMILES string
NC(Cc1c[nH]c2cccc(F)c12)C(O)=O
InChI key
DEBQMEYEKKWIKC-UHFFFAOYSA-N
assay
≥98.0% (TLC)
form
crystalline
technique(s)
NMR: suitable
color
off-white
storage temp.
−20°C
Biochem/physiol Actions
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.
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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 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 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.
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
Q S Zhang et al.
Journal of protein chemistry, 18(2), 187-192 (1999-05-20)
Escherichia coli 4-fluorotryptophan-substituted arginyl-tRNA synthetase was biosynthetically prepared and purified from a tryptophan auxotroph which could overproduce this enzyme. A method was developed to separate 4-fluorotryptophan from tryptophan and to determine accurately their contents in the 4-fluorotryptophan-containing proteins. It was
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