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Factors Affecting Solubility04:01

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Compared with pure water, the solubility of an ionic compound is less in aqueous solutions containing a common ion (one also produced by dissolution of the ionic compound). This is an example of a phenomenon known as the common ion effect, which is a consequence of the law of mass action that may be explained using Le Chȃtelier’s principle. Consider the dissolution of silver iodide:
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The soundness of cement refers to the ability of cement paste to retain its volume after setting. Unsound cement can lead to expansion and structural damage due to the presence of free lime, magnesia, and calcium sulfate. Free lime hydrates very slowly, expanding and causing unsoundness, which is difficult to detect because it intercrystallizes with other compounds. Magnesia also reacts with water, forming crystals that can disrupt the cement's structure. Calcium sulfate can create...
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Accelerators in concrete serve as admixtures to speed up the hardening process, enabling the concrete to achieve early strength faster. Although accelerators do not necessarily impact the time it takes concrete to set, they reduce this time in practice. A common accelerator is calcium chloride, which is particularly useful for hastening early strength development in cold weather or for rapid repair jobs that require quick heat generation after mixing.
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Drying Shrinkage01:21

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When hardened concrete is exposed to air with a relative humidity of less than 100 percent, it begins to lose the free water within its capillaries. As this water evaporates, the water initially adsorbed onto the calcium silicate hydrates migrates towards these now empty spaces and eventually evaporates as well. Over time, as more water leaves, the volume of the concrete decreases, a phenomenon known as drying shrinkage.
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The alkali-aggregate reaction in concrete involves natural siliceous minerals in aggregates reacting with alkaline hydroxides derived from cement alkalis. This reaction forms an alkali-silica gel that absorbs water, swells, and increases in volume, which is confined by the surrounding cement paste, creating internal pressures that crack and disrupt the concrete. The extent of expansion and damage can be partly attributed to the alkali-silica reaction's osmotic hydraulic pressure and the...
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Structure and function of rotavirus nonstructural protein NSP3

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Archives of Virology. Supplementum
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Rotavirus non-structural protein 3 (NSP3) binds to viral messenger RNAs, specifically recognizing the GACC sequence. This interaction is crucial for understanding rotavirus replication and its role within the Reoviridae family.

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Area of Science:

  • Virology
  • Molecular Biology
  • Genetics

Background:

  • Reoviridae viruses possess segmented double-stranded RNA genomes with conserved 5' and 3' end motifs.
  • These motifs are hypothesized to be involved in genomic segment assortment during virus assembly.
  • Identifying viral proteins that interact with RNA is key to understanding viral replication mechanisms.

Purpose of the Study:

  • To identify rotavirus proteins that bind to viral RNA during infection.
  • To characterize the RNA-binding specificity of the non-structural protein 3 (NSP3).
  • To elucidate the role of NSP3 in rotavirus replication.

Main Methods:

  • Utilized monoclonal antibodies (MAbs) to precipitate RNA-protein complexes from infected cells.
  • Employed in vitro RNA labeling and RNase T1 digestion to analyze protected RNA sequences.
  • Expressed recombinant NSP3 in a baculovirus-insect cell system for in vitro binding studies.

Main Results:

  • Demonstrated that NSP3 binds to all eleven rotavirus messenger RNAs in infected cells.
  • Identified a specific RNA sequence (nucleotides 8-15) protected by NSP3 from RNase T1 digestion.
  • Determined the minimal binding sequence for NSP3 in vitro to be GACC.

Conclusions:

  • NSP3 plays a significant role in rotavirus replication through specific RNA binding.
  • The GACC sequence is a critical determinant for NSP3-RNA interaction.
  • Findings contribute to understanding RNA-binding proteins in the Reoviridae family.