The types of amino acids that significantly contribute to evolutionary rates can be grouped into GC-rich and AT-rich amino acids. Besides, the amino acid with high composition also contributes more to evolutionary rates than amino acid with low composition in proteome. In summary, amino acid ...
Intrinsically disordered proteins and protein regions (IDPs) are prevalent in all proteomes and are essential to cellular function. Unlike folded proteins, IDPs exist in an ensemble of dissimilar conformations. Despite this structural plasticity, intramo
Jones DD. Amino acid properties and side-chain orientation in proteins:a cross correlation approach[J].Journal of Theoretical Biology,1975.167-183.Jones DD. Amino acid properties and side-chain orientation in proteins: a cross correlation approach. J Theor Biol 1975; 50:167-83....
We considered the hypothesis that some of this effect could be explained by TRNAU1AP indirectly regulating splicing events through modulating the splicing of other splicing factors. This multi-layered control of splicing has been shown in the recently characterized splicing factor DAP3 (ref. 52) as...
The primary structure consists of the amino acid sequence of the protein. Even at this level, there is substantial biochemical complexity including the acidity, size, hydrophobicity, and charge conferred by the different amino acids. Regarding acidity, there are three types of amino acids; neutral ...
Finally, we conclude that the abundance and amino acid composition of LCRs in P. falciparum can be explained primarily by this organism's highly A+T biased genome and its high recombination rate. Access through your organization Check access to the full text by signing in through your ...
However, it is not clear which amino acids are involved. On one hand, cod and soy proteins contain higher arginine levels than casein [16]. At levels found in dietary proteins, arginine is associated with a decrease of plasma insulin and the insulin/glucagon ratio [17]. This suggests that...
Gene regulation in bacteriophage λ is controlled by a key component, the λcI repressor that acts as a genetic switch between the lysogenic growth and lytic development [30,31]. cI is a protein formed by 236 amino acids distributed in two domains. In a lysogenic state, the host is not ...
For the three dynein heavy chains, comprising 13,382 amino acids in all, we observed a total of 155 intramolecular cross-links (Fig. 2a). This large number of intramolecular cross-links may be explained by the enrichment of dynein heavy chains in the endogenous sample and high-concentration ...
Subpopulations of soluble, misfolded proteins can bypass chaperones within cells. The extent of this phenomenon and how it happens at the molecular level are unknown. Through a meta-analysis of the experimental literature we find that in all quantitative