ArticleBiophysical journal2014
The effects of thermal disorder on the solution-scattering profiles of macromolecules.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Small-angle X-ray scattering profile calculation for high-resolution models of biomacromolecules.Journal of applied crystallography · 2025Article
- Fitting high-resolution electron density maps from atomic models to solution scattering data.Biophysical journal · 2023Article
- Refining conformational ensembles of flexible proteins against small-angle x-ray scattering data.Biophysical journal · 2021Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- Predicting X-ray solution scattering from flexible macromolecules.Protein science : a publication of the Protein Society · 2018Article
- Article
- WAXSiS: a web server for the calculation of SAXS/WAXS curves based on explicit-solvent molecular dynamics.Nucleic acids research · 2015Article
- Interpretation of solution x-ray scattering by explicit-solvent molecular dynamics.Biophysical journal · 2015Article
- Emerging applications of small angle solution scattering in structural biology.Protein science : a publication of the Protein Society · 2015Review
- Accurate small and wide angle x-ray scattering profiles from atomic models of proteins and nucleic acids.The Journal of chemical physics · 2014Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The solution-scattering profiles of macromolecules are significantly affected by the thermal motions of their atoms, especially at wide scattering angles, even when only a single conformational state is significantly populated in solution. Here it is shown that the impact thermal motions have on the molecular component of the solution-scattering profile of a single-state macromolecule can be predicted accurately if the variances and covariances of the thermal excursions of its atoms from their average positions are known.
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