ArticleBioinformatics and biology insights2010
Normal Mode Flexible Fitting of High-Resolution Structures of Biological Molecules Toward SAXS Data.
Article in Bioinformatics and biology insights, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Reconstruction of Three-Dimensional Conformations of Bacterial ClpB from High-Speed Atomic-Force-Microscopy Images.Frontiers in molecular biosciences · 2021Article
- Article
- Editorial: Hybrid Biomolecular Modeling.Frontiers in molecular biosciences · 2018Article
- Modeling macromolecular motions by x-ray-scattering-constrained molecular dynamics.Biophysical journal · 2015Article
- Article
- Developing advanced X-ray scattering methods combined with crystallography and computation.Methods (San Diego, Calif.) · 2013Review
- Integrative structural modeling with small angle X-ray scattering profiles.BMC structural biology · 2012Review
- Accurate flexible fitting of high-resolution protein structures to small-angle x-ray scattering data using a coarse-grained model with implicit hydration shell.Biophysical journal · 2011Article
- Solution structure of RNase P RNA.RNA (New York, N.Y.) · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present a method to reconstruct a three-dimensional protein structure from an atomic pair distribution function derived from the scattering intensity profile from SAXS data by flexibly fitting known x-ray structures. This method uses a linear combination of low-frequency normal modes from an elastic network description of the molecule in an iterative manner to deform the structure to conform optimally to the target pair distribution function derived from SAXS data. For computational efficiency, the protein and water molecules included in the protein first hydration shell are coarse-grained. In this paper, we demonstrate the validity of our coarse-graining approach to study SAXS data. Illustrative results of our flexible fitting studies on simulated SAXS data from five different proteins are presented.
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