857246

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Design of a bacterial host for site-specific incorporation of p-bromophenylalanine into recombinant proteins.

Inchan Kwon et al.

Journal of the American Chemical Society, 128(36), 11778-11783 (2006-09-07)

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 to amber stop codons. However, high-fidelity incorporation

Thermal neutron capture therapy: the Japanese-Australian clinical trial for malignant melanoma.

B J Allen et al.

Basic life sciences, 50, 69-73 (1989-01-01)

Neutron capture therapy for melanoma.

J A Coderre et al.

Basic life sciences, 50, 219-232 (1989-01-01)

Dose fractionation in neutron capture therapy for malignant melanoma.

B J Allen et al.

Basic life sciences, 50, 63-67 (1989-01-01)

Efficient introduction of aryl bromide functionality into proteins in vivo.

N Sharma et al.

FEBS letters, 467(1), 37-40 (2000-02-09)

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, however, by the availability of just the

Controlling enzyme inhibition using an expanded set of genetically encoded amino acids.

Shun Zheng et al.

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

Fluorescence quenching in a strongly helical peptide series: the role of noncovalent pathways in modulating electronic interactions.

G Basu et al.

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

Relaxing the substrate specificity of an aminoacyl-tRNA synthetase allows in vitro and in vivo synthesis of proteins containing unnatural amino acids.

M Ibba et al.

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

Structural plasticity of an aminoacyl-tRNA synthetase active site.

James M Turner et al.

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

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