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- W137344068 abstract "The ability to predict electrostatic contributions to protein stability from structure has been a long-standing goal of experimentalists and theorists. With recent advances in NMR spectroscopy, it is possible to determine pKa values of all ionizable residues for at least small proteins, and to use the pKa shift between the folded and unfolded states to calculate the thermodynamic contribution from a change in charge to the change in free energy of unfolding. Results for globular proteins and for α-helical coiled coils show that electrostatic contributions to stability are typically small on an individual basis, particularly for surface-exposed residues. We discuss why NMR often suggests smaller electrostatic contributions to stability than X-ray crystallography or site-directed mutagenesis, and discuss the type of information needed to improve structure-based modeling of electrostatic forces. Large pKa shifts from random coil values are observed for proteins bound to negatively charged sodium dodecyl sulfate micelles. The results suggest that electrostatic interactions between proteins and charges on the surfaces of membrane lipid bilayers could be a major driving force in stabilizing the structures of peripheral membrane proteins. Finally, we discuss how changes in ionization states affect amyloid-β fibril formation and suggest that electrostatic repulsion may be a common destabilizing force in amyloid fibrils." @default.
- W137344068 created "2016-06-24" @default.
- W137344068 creator A5033187058 @default.
- W137344068 creator A5056376832 @default.
- W137344068 creator A5065812817 @default.
- W137344068 creator A5069765122 @default.
- W137344068 date "2009-01-01" @default.
- W137344068 modified "2023-09-27" @default.
- W137344068 title "Electrostatic Contributions to the Stabilities of Native Proteins and Amyloid Complexes" @default.
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- W137344068 doi "https://doi.org/10.1016/s0076-6879(09)66010-9" @default.
- W137344068 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21609864" @default.
- W137344068 hasPublicationYear "2009" @default.
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