The HIV-1 genome and the structural proteins derived from the gag gene. This ability plays a fundamental role in the HIV-1 replication and reverse transcriptase processes.
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Figure 3. The zinc binding motifs provide stabilization for the small protein. DOI: Very small protein domains often require some sort of structural stabilization, which can often be accomplished through the binding of metal ions. Figure 4.
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The cysteine and histidine residues that chelate zinc are shown in gray. The numbers 16 and 37, highlight the hydrophobic residues for each zinc finger, that are utilized for RNA binding. Adapted from Levin, Each Zn finger contains an aromatic, hydrophobic residue: this is phenylalanine 16 F in the N-terminal Zn finger and tryptophan 37 W in the C-terminal Zn finger, shown in Figure 2.
In a mature HIV-1 retrovirus, the aromatic residues from the two Zn fingers are found side by side, as a result of the the flexibility of the peptide linker. This hydrophobic patch provides an ideal platform for RNA binding through stacking interactions with residues in RNA nucleic acid sequences, shown in FIgure 5 below. Figure 5. This psi site has four different stem loops SL1-SL4. Each zinc-finger domain is a tetradentate ligand, binding to Zn with three cysteine sulfur atoms, and one histidine imidazole nitrogen.
The interaction between each Zn finger domain and its Zn metal ion is particularly stable, with affinity of approximately [can you find affinities anywhere? The stability and selectivity of these interactions can be explained by several principles of inorganic chemistry, described below. The three cysteines and one histidine residue provide four coordinating ligands for Zn and they are also connected by the protein backbone or by peptide bonds.
This makes the Zn finger domain a multi-dentate ligand. A multidentate ligand, or in other words a chelator, is a ligand that binds to a metal ion through more than one donor group.
This leads to a tetradentate complex that is more thermodynamically stable than an analogous complex of Zn with individual C,C,C,and H amino acids. The increased stability is due to the chelate effect, which is fundamentally explained by an increase in entropy. To illustrate the chelate effect, imagine a reaction that begins with two molecules on the reactants side, the protein CCHC and the hydrated Zn metal.
However, upon completion of the reaction, the water molecules attached to the Zn ion are replaced with the chelator, resulting in an increase of total molecules to five, as shown in Figure 6 below. The increase in molecules from reactants to products results in an increase in entropy. This increase in entropy is favorable, and therefore, the Zn-CCHC complex has increased stability due to this chelate effect.
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Figure 6. The numbers show that the reaction encourages an increase in molecules, indicating an increase in entropy. This increase in entropy provides a more thermodynamically stable metal-ligand complex, and therefore, is more favorable. C Corresponding author. Email: pmsmith plants. Southern analysis and sequencing of genomic DNA confirmed that these differences result from alternative splicing of the primary transcript of a single Vupur3 gene. Alternative splicing does not appear to play a role in the production of soybean Glycine max Merrill. The presence of the protein product of the Vupur3 gene, GART, in plastids and mitochondria was confirmed by immunoblotting with antibodies raised against the recombinant protein.
From the journal: Chemical Communications. Sarah R.
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