title: Dynamic contributions to the DNA binding entropy of the EcoRI and EcoRV restriction endonucleases.
abstract: Molecular Dynamics simulations on DNA-EcoRI and DNA-EcoRV complexes suggest that the DNA within these complexes is significantly more ordered than free DNA. Similarly, both the protein and the DNA are more ordered in the specific (cognate) DNA-EcoRV complex than they are in the non-cognate DNA-protein complex, consistent with recently proposed analogies between protein folding and sequence-specific DNA-protein recognition. Analysis of the trajectories shows that the net entropy gain upon specific binding to be the result of opposing contributions. Solvent release, which increases entropy versus configurational terms (as measured by the magnitude of the atomic fluctuations), and collective terms from tight coupling between the motions of the protein and the DNA.
authors.affiliation: Department of Biological Sciences, University of Pittsburgh, PA 15260, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Duan
authors.forename: P
authors.initials: P
authors.lastname: Wilkosz
authors.forename: J M
authors.initials: JM
authors.lastname: Rosenberg
mesh_terms: D003198:Computer Simulation; D004247:DNA / Q000737:chemistry*; D015246:Deoxyribonuclease EcoRI / Q000737:chemistry*; D015252:Deoxyribonucleases, Type II Site-Specific / Q000737:chemistry*; D019277:Entropy; D008969:Molecular Sequence Data; D011485:Protein Binding
chemical_list: D004247:DNA; D015246:Deoxyribonuclease EcoRI; D015252:Deoxyribonucleases, Type II Site-Specific; C027440:GATATC-specific type II deoxyribonucleases