Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water
- 13 October 2017
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 358 (6360) , 238-241
Abstract
An expanded view of disordered proteins: Disordered proteins sample an ensemble of conformations, but it has remained unclear how compact these conformations are in water. Polymer physics relates the radius of gyration ( R g ) to solvent quality, with more chain collapse occurring in poorer solvents. Riback et al. developed an analysis scheme that allows them to extract solvent quality and R g from a single small-angle x-ray scattering measurement. Applying this method, they found that even disordered proteins with low net charge and high hydrophobicity remain expanded in water. Science , this issue p. 238Keywords
Funding Information
- National Science Foundation (award343915, GRF DGE-1144082)
- National Science Foundation (award343916, MCB 1516959)
- National Institutes of Health (award343921, 1S10OD018090-01)
- National Institute of General Medical Sciences (award343917, GM055694)
- National Institute of General Medical Sciences (award343918, GM055694)
- National Institute of General Medical Sciences (award343920, GM103622)
- National Institute of General Medical Sciences (award343919, GM097573)
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