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Quality Level
Assay
99%
form
powder
reaction suitability
reaction type: solution phase peptide synthesis
mp
262-263 °C (dec.) (lit.)
application(s)
peptide synthesis
storage temp.
2-8°C
SMILES string
NC(Cc1ccc(Br)cc1)C(O)=O
InChI
1S/C9H10BrNO2/c10-7-3-1-6(2-4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)
InChI key
PEMUHKUIQHFMTH-UHFFFAOYSA-N
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Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Dose fractionation in neutron capture therapy for malignant melanoma.
Basic life sciences, 50, 63-67 (1989-01-01)
Biochemistry, 32(12), 3067-3076 (1993-03-30)
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-L-phenylalanine. The fluorescence of the
Proceedings of the National Academy of Sciences of the United States of America, 103(17), 6483-6488 (2006-04-19)
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 Methanococcus jannaschii tyrosyl aminoacyl-tRNA
FEBS letters, 364(3), 272-275 (1995-05-15)
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 machinery of Escherichia coli is
Biotechnology and bioengineering, 110(9), 2361-2370 (2013-04-10)
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 affecting enzyme substrate binding is often
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