Strong non-ideality effects at low protein concentrations: considerations for elongated proteins
Author:
Funder
National Institute of General Medical Sciences
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
https://link.springer.com/content/pdf/10.1007/s00249-023-01648-x.pdf
Reference63 articles.
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2. Brautigam CA, Tso S-C, Deka RK, Liu WZ, Norgard MV (2020) Using modern approaches to sedimentation velocity to detect conformational changes in proteins. Eur Biophys J 49:729–743. https://doi.org/10.1007/s00249-020-01453-w
3. Brookes E, Demeler B, Rosano C, Rocco M (2010) The implementation of somo (solution modeller) in the ultrascan analytical ultracentrifugation data analysis suite: Enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule. Eur Biophys J 39:423–435. https://doi.org/10.1007/s00249-009-0418-0
4. Bujacz A (2012) Structures of bovine, equine and leporine serum albumin. Acta Crystallogr D Biol Crystallogr 68:1278–1289. https://doi.org/10.1107/s0907444912027047
5. Byron O (1997) Construction of hydrodynamic bead models from high-resolution X-ray crystallographic or nuclear magnetic resonance data. Biophys J 72:408–415. https://doi.org/10.1016/S0006-3495(97)78681-8
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