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Multi-scale calculation and global-fit analysis of hydrodynamic properties of biological macromolecules: determination of the overall conformation of antibody IgG molecules
- Source :
- European Biophysics Journal. 39:361-370
- Publication Year :
- 2008
- Publisher :
- Springer Science and Business Media LLC, 2008.
-
Abstract
- We present a scheme, based on existing and newly developed computational tools, for the determination of the overall conformation of biological macromolecules composed by domains or subunits, using from such structural determination easily available solution properties. In a multi-scale approach, atomic-level structures are used to provide simple shapes for the subunits, which are put together in a coarse grained model, with a few parameters that determine the overall shape of the macromolecule. Computer programs, like those in the HYDRO suite that evaluate the properties of either atomic or coarse-grained models. In this paper we present a new scheme for a global fit of multiple properties, implemented in a new computer program, HYDROFIT, which interfaces with the programs of the HYDRO suite to find an optimum, best-fitting structure in a robust but simple way. The determination of the overall structure of the native antibody IgG3, bearing a long hinge, and that of the hingeless mutant m15 is presented to test and confirm the validity of this simple, systematic and efficient scheme.
- Subjects :
- Fit/gap analysis
Computer program
Scale (ratio)
Computers
Protein Conformation
Chemistry
Biophysics
Hinge
Water
Nanotechnology
General Medicine
Immunoglobulin Fc Fragments
Immunoglobulin Fab Fragments
Models, Chemical
Simple (abstract algebra)
Immunoglobulin G
Mutation
Molecule
Biological system
Software
Macromolecule
Subjects
Details
- ISSN :
- 14321017 and 01757571
- Volume :
- 39
- Database :
- OpenAIRE
- Journal :
- European Biophysics Journal
- Accession number :
- edsair.doi.dedup.....d148a2a4de468288223053336571b247