Solution structure of biopolymers: A new method of constructing a bead model

We propose a new, automated method of converting crystallographic data into a bead model used for the calculations of hydrodynamic properties of rigid macromolecules. Two types of molecules are considered: nucleic acids and s mall proteins. A bead model of short DNA fragments has been constructed in which each nucleotide is represented by two identical, partially overlappin g spheres: one for the base and one for the sugar and phosphate group. The optimum radius sigma = 5.0 Angstrom was chosen on the basis of a comparison of the calculated translational diffusion coefficients (D-T) and the rotat ional relaxation times (tau(R)) with the corresponding experimental data fo r B-DNA fragments of 8, 12, and 20 basepairs. This value was assumed for th e calculation D-T and tau(R) of tRNA(Phe). Better agreement with the experi mental data was achieved for slightly larger sigma = 5.7 Angstrom. A simila r procedure was applied to small proteins. Bead models were constructed suc h that each amino acid was represented by a single sphere or a pair of iden tical, partially overlapping spheres, depending on the amino acid's size. E xperimental data of D-T of small proteins were used to establish the optimu m value of sigma = 4.5 Angstrom for amino acids. The lack of experimental d ata on tau(R) for proteins restricted the tests to the translational diffus ion properties.