An overview of protein-DNA and protein-RNA interactions

In this review the fundamental question of how does protein-DNA or protein-RNA interactions affect the structures and dynamics of DNA, RNA, and protein is addressed. Two models of human serum albumin (HSA) bindings to calf-thymus DNA and transfer RNA ( tRNA) are presented here. In these models the binding sites, stability and structural aspects of DNA-protein and RNA-protein are discussed. Electrostatic binding of DNA or RNA via backbone phosphate group to the positively charged amino acids on the surface of protein is prevailing. Two binding sites with K-1 = 4.8 x 10(5) M-1 and K-2 = 6.1 x 10(4) M-1 for protein-DNA and one binding affinity with K = 1.45 x 10(4) M-1 for protein-RNA are observed. A partial B to A-DNA transition is observed for protein-DNA complexes, while tRNA remains in A-family structure upon protein interaction.