Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models.

ABSTRACT: Here we extend the ability to predict hydrodynamic coefficients and other solution properties of rigid macromolecular structures from atomic-level structures, implemented in the computer program HYDROPRO, to models with lower, residue-level resolution. Whereas in the former case there is one bead per nonhydrogen atom, the latter contains one bead per amino acid (or nucleotide) residue, thus allowing calculations when atomic resolution is not available or coarse-grained models are preferred. We parameterized the effective hydrodynamic radius of the elements in the atomic- and residue-level models using a very large set of experimental data for translational and rotational coefficients (intrinsic viscosity and radius of gyration) for >50 proteins. We also extended the calculations to very la

SUBMITTER: Ortega A 

PROVIDER: S-EPMC3175065 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature