- Inverted solubility--melting a crystal by cooling--is observed in a handful of proteins, such as carbomonoxy hemoglobin and gammaD-crystallin. In human gammaD-crystallin, the phenomenon is associated with the mutation of the 23rd residue, a proline, to a threonine, serine or valine. One proposed microscopic mechanism entails an increase in surface hydrophobicity upon mutagenesis. Recent crystal structures of a double mutant that includes the P23T mutation allow for a more careful investigation of this proposal. Here, we first measure the surface hydrophobicity of various mutant structures of gammaD-crystallin and discern no notable increase in hydrophobicity upon mutating the 23rd residue. We then investigate the solubility inversion regime with ... [Read More]
- Total Size
- 113 files (21.8 MB)
- Data Citation
- Altan, I., James, S., Khan, A., Quinn, M., Charbonneau, P., & McManus, J. (2019). Data and scripts from: Using Schematic Models to Understand the Microscopic Basis for Inverted Solubility in gammaD-crystallin. Duke Digital Repository. https://doi.org/10.7924/r4fq9v942
- Creator
- DOI
- 10.7924/r4fq9v942
- Publication Date
- September 30, 2019
- ARK
- ark:/87924/r4fq9v942
- Affiliation
- Publisher
- Type
- Related Materials
- Contact
- Patrick Charbonneau; patrick.charbonneau@duke.edu, ORCID: 0000-0001-7174-0821
- Title
- Data and scripts from: Using Schematic Models to Understand the Microscopic Basis for Inverted Solubility in gammaD-crystallin
- Repository
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