Analysis of cation–π interactions to the structural stability of RNA binding proteins

Distinct role of non-covalent interactions to the function and structural stability of glutaredoxins: a multifunctional redox protein

“…By calculating the range of these energies, we have depicted the results in Figures 5 and 6, which shows that most of the energetically significant cation-л interaction residues have energy between −3 and −5 kcal/mol, which is in accordance with the earlier stated energy range of significant cation-л interactions in RNA binding proteins (Chakkaravarthi and Gromiha, 2006). From this, we infer that these interactions play a significant role in the structural stability and function of glutaredoxins.…”

“…Also, the importance of cation-л interactions as an important non-covalent binding interaction in structural biology is already established (Gallivan and Dougherty, 1999;Dougherty, 1996). Many investigators have stated the significance of these interactions in folding of polypeptides (Shi et al, 2002), helicity of α-helical peptides (Shi et al, 2002), determination of protein structure (Gallivan and Dougherty, 2000), biomolecular association (Novotny et al, 1989;Pellequer et al, 2000;Dougherty and Stauffer, 1990;Mecozzi et al, 1996) and in stability of various proteins (Gromiha and Suwa, 2005;Gromiha, 2003;Gromiha et al, 2004Gromiha et al, , 2002Chakkaravarthi and Gromiha, 2006;Chakravarthy and Varadarajan, 2000). In addition, another type of non-covalent interaction, i.e., CH…л interaction, is getting more and more emphasised in the fields of biochemistry and biophysical chemistry and they are considered as an important interaction in the stability of three-dimensional protein structure (Shanthi et al, 2009).…”

A thorough anion–π interaction study in biomolecules: on the importance of cooperativity effects

“…Similarly, several cation–π studies by Gromiha and coworkers show that Arg has a higher preference to form cation–π interactions than Lys and that the roles of these cation–π interactions are different from other noncovalent contacts in the stability of protein structures. 46 – 48 …”

Influence of cation-π interactions on RNA-binding proteins

“…The work of Morozova et al [17], mainly focused on the stacking of arginine with adenine, cytosine and uracil with respect to RNA recognition. Also, a recent report on the analysis of cation-interactions to the structural stability RNAbinding proteins [18] have made use of 51 RNA binding protein IDs out which 37% did not show any cation-interactions. Hence, we thought of excluding those 41 PDB ID's used in [17] and the 51 PDB ID's used in [18] and selected a separate set of 37 RNA binding proteins which are completely nonoverlapping with the IDs' reported in [17,18] our data set showed significant cation-interactions and hence we believe that this investigation should be statistically more significant.…”