Determining Rg of IDPs from SAXS Data
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Publisher
Springer US
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http://link.springer.com/content/pdf/10.1007/978-1-0716-0524-0_13
Reference26 articles.
1. Das RK, Pappu RV (2013) Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proc Natl Acad Sci U S A 110:13392–13397. https://doi.org/10.1073/pnas.1304749110
2. Hoffmann A, Kane A, Nettels D et al (2007) Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy. Proc Natl Acad Sci U S A 104:105–110. https://doi.org/10.1073/pnas.0604353104
3. Hofmann H, Soranno A, Borgia A et al (2012) Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy. Proc Natl Acad Sci U S A 109:16155–16160. https://doi.org/10.1073/pnas.1207719109
4. Mao AH, Crick SL, Vitalis A et al (2010) Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci U S A 107:8183–8188. https://doi.org/10.1073/pnas.0911107107
5. David G, Perez J (2009) Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the synchrotron SOLEIL SWING beamline. J Appl Crystallogr 42:892–900. https://doi.org/10.1107/s0021889809029288
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