Analysis of accessible surface of residues in proteins

摘要: We analyzed the total, hydrophobic, and hydrophilic accessible surfaces (ASAs) of residues from a nonredundant bank 587 3D structure proteins. In an extended fold, are classified into three families with respect to their hydrophobicity balance. As expected, lose part solvent-accessible surface folding but groups remain. The decrease accessibility is more pronounced for hydrophobic than residues. Amazingly, Lysine residue largest in folded structures. Our analysis points out clear difference between mean (other studies) median (this study) ASA values residues, which should be taken consideration future investigations on protein-accessible surface, order improve predictions requiring values. different secondary structures correspond Random coils, turns, β-structures (outside β-sheets) most folds, average 30% accessibility. helical about 20% accessible, illustrates amphipathy many helices. Residues β-sheets inaccessible solvent (10% accessible). Hence, appropriate shield parts water. also show that there equal balance protein irrespective size. This results patchwork areas, could important interactions and/or activity.