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In structural biology, a heterologous association is a binding mode between the protomers of a protein structure. [3] In a heterologous association, each protomer contributes a different set of residues to the binding interface.
Heterologous expression refers to the expression of a gene or part of a gene in a host organism that does not naturally have the gene or gene fragment in question. Insertion of the gene in the heterologous host is performed by recombinant DNA technology .
In many plants, defensive or storage structures are made by modifications of the development of primary leaves, stems, and roots. Leaves are variously modified from photosynthetic structures to form the insect-trapping pitchers of pitcher plants, the insect-trapping jaws of the Venus flytrap, and the spines of cactuses, all homologous. [35]
The K Homology (KH) domain is a protein domain that was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K.An evolutionarily conserved sequence of around 70 amino acids, the KH domain is present in a wide variety of nucleic acid-binding proteins.
More recently, Myceliophthora thermophila C1 has been developed into an expression platform for screening and production of native and heterologous proteins.The expression system C1 shows a low viscosity morphology in submerged culture, enabling the use of complex growth and production media.
The enzyme from Escherichia coli consists of two alpha8-beta8 (TIM) barrels positioned face to face and thought to have evolved by gene duplication. [1] The active site lies between the tops of the two barrels, the N-terminal barrel binds 5-methyltetrahydropteroyltri-L-glutamic acid and the C-terminal barrel binds homocysteine.
Once the heterologous protein has been fused with the bacterial cell surface protein, it is exposed to either an enzyme, a cell (expressing a target protein) or an antibody (usually fluorescently tagged), depending on the application of the experiment. The sample is then passed through a beam of light during FACS, in a very narrow stream of ...
Because this enrichment is so pronounced, the enzyme is hypothesized to produce (+)-pinoresinol exclusively, and to compete with the non-protein-mediated coupling reaction, which produces a heterologous mix of products. [9] This has been confirmed by analyzing the various mixtures produced with different concentrations of dirigent proteins present.