An overview of protein-DNA and protein-RNA interactions

Autor:	H. A. Tajmir-Riahi
Rok vydání:	2006
Předmět:	chemistry.chemical_compound A-site chemistry HMG-box Biochemistry Binding protein Transfer RNA RNA General Chemistry Binding site DNA Binding domain
Zdroj:	Journal of the Iranian Chemical Society. 3:297-304
ISSN:	1735-2428 1735-207X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::d93f1a650a67d2ff2561699b00105e6a https://doi.org/10.1007/bf03245950 Zobrazit plný text záznamu Full text from SpringerLink