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Such structural data makes these proteins particularly suitable for prioritization of structure-based drug design strategies.

The essential requirement of ferritins/bacterioferritins (proteins involved in iron storage and homeostasis) for the survival of several prokaryotic pathogens makes these proteins very attractive targets for structure determination and inhibitor design.

The almost complete loss of dsRNA cleavage activity of R39A/G38D and Q28A/G38D/R39A can be explained by the absence of Arg39 which makes these proteins poor in melting the helix, and the presence of aspartic acid at position 38 which results in a compromised flexibility of the protein.

This hypervariability makes these proteins difficult to study and their primary function(s) remain to be discovered.

14, 15 The involvement of a variety of Ras superfamily proteins in human tumorigenesis makes these proteins interesting subjects in cancer research, and hence, the identification and functional characterization of novel GTPases is an important topic in molecular cell biology.

We focused on these classes because they mediate male female post-mating interactions in Drosophila and are rapidly evolving, which makes these proteins likely to be involved in sexual conflict [ 82, 83].

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Such dissimilarities make these proteins very interesting for drug design and molecular intervention.

When, and only when, these genes are turned on do the bacteria make these proteins and light up.

Immunotoxin expressed in C. reinhardtii chloroplasts by Tran et al. (2013b), binds target B-cells and kills them, making these proteins potential cancer therapies.

While they are completely absent in mammalians, they are key players in the survival of disease-causing protozoans making these proteins attractive pharmacological targets.

Researchers have used chemical synthesis and genetic methods to make these proteins and more: protein catenanes, neoglycoproteins, and artificial protein molecules with novel architectures or made from novel building blocks.

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