ArticleBiopolymers2011
X-ray solution scattering studies of the structural diversity intrinsic to protein ensembles.
Article in Biopolymers, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Biophysical Approaches for the Characterization of Protein-Metabolite Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Mechanisms of isoform-specific residue influence on GTP-bound HRas, KRas, and NRas.Biophysical journal · 2022Article
- Predicting X-ray solution scattering from flexible macromolecules.Protein science : a publication of the Protein Society · 2018Article
- The role of small-angle scattering in structure-based screening applications.Biophysical reviews · 2018Review
- Article
- Sulfmyoglobin Conformational Change: A Role in the Decrease of Oxy-Myoglobin Functionality.Biochemistry and biophysics reports · 2016Article
- Modulation of HIV protease flexibility by the T80N mutation.Proteins · 2015Article
- New look at hemoglobin allostery.Chemical reviews · 2015Review
- The effects of thermal disorder on the solution-scattering profiles of macromolecules.Biophysical journal · 2014Article
- Wide-angle X-ray solution scattering for protein-ligand binding: multivariate curve resolution with Bayesian confidence intervals.Biophysical journal · 2013Article
- Biophysical and structural characterization of a sequence-diverse set of solute-binding proteins for aromatic compounds.The Journal of biological chemistry · 2012Article
- Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100 ps to 10 ms with pump-probe X-ray solution scattering.Journal of the American Chemical Society · 2012Article
- How random are intrinsically disordered proteins? A small angle scattering perspective.Current protein & peptide science · 2012Review
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7 authors.
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Abstract
It is becoming increasingly clear that characterization of the protein ensemble-the collection of all conformations of which the protein is capable-will be a critical step in developing a full understanding of the linkage between structure, dynamics, and function. X-ray solution scattering in the small angle (SAXS) and wide-angle (WAXS) regimes represents an important new window to exploring the behavior of ensembles. The characteristics of the ensemble express themselves in X-ray solution scattering data in predictable ways. Here we present an overview of the effect that structural diversity intrinsic to protein ensembles has on scattering data. We then demonstrate the observation of these effects in scattering from four molecular systems; myoglobin; ubiquitin; alcohol dehydrogenase; and HIV protease; and demonstrate the modulation of these ensembles by ligand binding, mutation, and environmental factors. The observations are analyzed quantitatively in terms of the average spatial extent of structural fluctuations occurring within these proteins under different experimental conditions. The insights which these analyses support are discussed in terms of the function of the various proteins.
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