TY - JOUR T1 - Netropsin binding to poly[d(IC)].poly[IC)] and poly[d(GC].poly[d(GC)]: a computer simulation. JF - Molecular Pharmacology JO - Mol Pharmacol SP - 341 LP - 346 VL - 37 IS - 3 AU - F Gago AU - W G Richards Y1 - 1990/03/01 UR - http://molpharm.aspetjournals.org/content/37/3/341.abstract N2 - The thermodynamic cycle perturbation approach has been used to calculate the difference in the free energy of binding of netropsin to two different DNA molecules. In the computer simulations, all the inosine residues have been gradually 'mutated' into guanosine in a DNA dodecamer and in a complex of the same dodecamer with netropsin. The difference in binding free energy of about 4.3 kcal mol-1 agrees well with the experimentally determined value of 4.0 kcal mol-1. One structural determinant of the specificity seems to be the width of the minor groove in the two complexes. ER -