INTRODUCTION Protein thermostability is an important field for its evolutionary perspective of mesophilic versus thermophilic relationship and for its industrial/ therapeutic applications. METHODS Presently, a total 400 (200 thermophilic and 200 mesophilic homologue) proteins were studied utilizing several software/databases to evaluate their amino acid preferences. Randomly selected 50 homol...

Studies on collagen and collagen-like peptides suggest that triple-helical stability can vary along the amino acid chain. In this regard, it has been shown that lysine residues in the Y position and acidic residues in the X' position of (GPO)(3)GXYGX'Y'(GPO)(3) peptides lead to triple-helical structures with melting temperatures similar to (GPO)(8) (where O is hydroxyproline), which is generall...

The equilibrium dissociation constant of the DNA binding domain of interferon regulatory factor 1 (IRF1 DBD) for its DNA binding site depends strongly on salt concentration and salt type. These dependencies are consistent with IRF1 DBD binding to DNA, resulting in the release of cations from the DNA and both release of anions from the protein and uptake of a cation by the protein. We demonstrat...

NMR investigations have been carried out on the B1 domain of protein G. This protein has six lysine residues, of which three are consistently found to form surface-exposed salt bridges in crystal structures, while the other three are not. The Nzeta and Hzeta chemical shifts of all six lysines are similar and are not affected significantly by pH titration of the carboxylate groups in the protein...