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The oldest and most widely used expression systems are cell-based and may be defined as the "combination of an expression vector, its cloned DNA, and the host for the vector that provide a context to allow foreign gene function in a host cell, that is, produce proteins at a high level".
[81]: 163 This number is found by calculating the number of ways that 21 items (20 amino acids plus one stop) can be placed in 64 bins, wherein each item is used at least once. [82] However, the distribution of codon assignments in the genetic code is nonrandom. [83] In particular, the genetic code clusters certain amino acid assignments.
This applies to studies of single molecules within single cells to medium-throughput drug-screening applications. By screening oocytes for the expression of injected cDNA, the application of micro injection as a model for heterologous expression can be studied further in terms of cell signaling, transport, architecture, and protein function.
For a protein containing n amino acids, the number of high-energy phosphate bonds required to translate it is 4n-1. [9] The rate of translation varies; it is significantly higher in prokaryotic cells (up to 17–21 amino acid residues per second) than in eukaryotic cells (up to 6–9 amino acid residues per second). [10]
HIV-1 gp41 is used to bind chemokines on the cell surface of the host so that the virion may gain entrance into the host. Astrocytes are cells of the CNS which are used to regulate the concentrations of K + and neurotransmitter which enter the cerebrospinal fluid (CSF) to contribute to the blood brain barrier. A twelve amino acid sequence (Leu ...
They propagate themselves in host cells by making conformational changes in other molecules of protein with the same amino acid sequence, but with a different conformation that is functionally important or detrimental to the organism. Once the protein has been transconformed to the prion folding it changes function.
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Other key stimulatory factors were also found in the study. [1] Importin-β, unlike importin-α, has no direct homologues in yeast, but was purified as a 90-95 kDa protein and found to form a heterodimer with importin-α in a number of different cases. These included a study led by Michael Rexach [4] and further studies by Dirk Görlich. [5]