Non-polar nuclei in fungal microbial RNases

An application of a previously proposed method for the analysisof the non-polar structure of proteins is presented. A detailedanalysis of the composition and properties of non-polar nucleiand microclusters of fungal microbial ribonucleases has beenperformed on the basis of the 3-D structures of RNase T1 andrelated proteins. Three hydrophobic nuclei were found in thesestructures. It has been shown that all residues in non-polarnuclei have high homology ({small tilde}89%). Residues in thenuclei are practically fully buried in the interior of a molecule.Detailed analysis of non-polar nuclei properties shows thatthese nuclei determine the hydrophobic core of a protein andthe location and role of each residue in the non-polar interiorof proteins. In addition it was found that there are variableresidues not only on the surface of a protein but on the surfaceof the nuclei inside the protein and between the nuclei andthat there is a consistent region in all proteins, the hydrophobic-nuclei. An evaluation of the stability of non-polar nuclei,the conservation of their compositions and their positions inthe protein globule, allows one to assume that these three nucleiplay an important functional role in the stability and foldingof molecules of RNases and possibly can be considered as independentstructural elements of 3-D structures of these proteins.