 An Overview of Protein-DNA and Protein-RNA Interactions
Department of Chemistry-Biology, University of Québec at Trois-Rivières,C.P. 500, TR (Québec) Canada G9A 5H7H.A. Tajmir-Riahi 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 K1 = 4.8 × 105 M-1 and K2 = 6.1 × 104 M-1 for protein-DNA and one binding affinity with K = 1.45 × 104 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. Keywords: DNA, Protein, Binding mode, Binding constant, Secondary structure capillary electrophoresis, FTIR spectroscopy |
