4-Bromo-L-Phe-OH
4-Bromo-L-Phe-OH structure
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Common Name | 4-Bromo-L-Phe-OH | ||
|---|---|---|---|---|
| CAS Number | 14091-15-7 | Molecular Weight | 244.085 | |
| Density | 1.6±0.1 g/cm3 | Boiling Point | 368.4±32.0 °C at 760 mmHg | |
| Molecular Formula | C9H10BrNO2 | Melting Point | 262-263 °C (dec.)(lit.) | |
| MSDS | Chinese USA | Flash Point | 176.6±25.1 °C | |
| Symbol |
GHS07 |
Signal Word | Warning | |
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Efficient introduction of aryl bromide functionality into proteins in vivo.
FEBS Lett. 467(1) , 37-40, (2000) Artificial proteins can be engineered to exhibit interesting solid state, liquid crystal or interfacial properties and may ultimately serve as important alternatives to conventional polymeric materials. The utility of protein-based materials is limited, howev... |
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Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids.
FEBS Lett. 364(3) , 272-5, (1995) It has previously been demonstrated that the unnatural amino acid p-Cl-phenylalanine can be attached to tRNA(Phe) by a modified phenylalanyl-tRNA synthetase with relaxed amino acid substrate specificity. We show that this modification to the translational mac... |
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Neutron capture therapy for melanoma.
Basic Life Sci. 50 , 219-32, (1989)
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Thermal neutron capture therapy: the Japanese-Australian clinical trial for malignant melanoma.
Basic Life Sci. 50 , 69-73, (1989)
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Dose fractionation in neutron capture therapy for malignant melanoma.
Basic Life Sci. 50 , 63-7, (1989)
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Structural plasticity of an aminoacyl-tRNA synthetase active site.
Proc. Natl. Acad. Sci. U. S. A. 103(17) , 6483-8, (2006) Recently, tRNA aminoacyl-tRNA synthetase pairs have been evolved that allow one to genetically encode a large array of unnatural amino acids in both prokaryotic and eukaryotic organisms. We have determined the crystal structures of two substrate-bound Methano... |
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Design of a bacterial host for site-specific incorporation of p-bromophenylalanine into recombinant proteins.
J. Am. Chem. Soc. 128(36) , 11778-83, (2006) Introduction of a yeast suppressor tRNA (ytRNA(Phe)(CUA)) and a mutant yeast phenylalanyl-tRNA synthetase (yPheRS (T415G)) into an Escherichia coli expression host allows in vivo incorporation of phenylalanine analogues into recombinant proteins in response t... |
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Controlling enzyme inhibition using an expanded set of genetically encoded amino acids.
Biotechnol. Bioeng. 110(9) , 2361-70, (2013) Enzyme inhibition plays an important role in drug development, metabolic pathway regulation, and biocatalysis with product inhibition. When an inhibitor has high structural similarities to the substrate of an enzyme, controlling inhibitor binding without affe... |
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Fluorescence quenching in a strongly helical peptide series: the role of noncovalent pathways in modulating electronic interactions.
Biochemistry 32(12) , 3067-76, (1993) The very strong helical propensity of peptides rich in alpha-aminoisobutyric acid (Aib) has enabled the design of a set of helices containing as guest amino acids one fluorescent chromophore, beta-(1'-naphthyl)-L-alanine, and one heavy atom perturber, p-bromo... |