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 large proteins and macromolecular complexes, such as the whole 70S ribosome. We show that with proper parameterization, the two levels of resolution yield similar and rather good agreement with experimental data. The new version of HYDROPRO, in addition to considering various computational and modeling schemes, is far more efficient computationally and can be handled with the use of a graphical interface.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Ortega A,Amorós D,García de la Torre J

doi

10.1016/j.bpj.2011.06.046

subject

Has Abstract

pub_date

2011-08-17 00:00:00

pages

892-8

issue

4

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(11)00776-4

journal_volume

101

pub_type

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