ArticleProceedings of the National Academy of Sciences of the United States of America2007
Altered phase diagram due to a single point mutation in human gammaD-crystallin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 105 citations in OpenAlex.
- Quantitative Perspectives of Biomolecular Crystallization Thermodynamics.Advances in biochemical engineering/biotechnology · 2026Review
- Assembling membraneless organelles from de novo designed proteins.Nature chemistry · 2024Article
- The Relationship between Protein-Protein Interactions and Liquid-Liquid Phase Separation for Monoclonal Antibodies.Molecular pharmaceutics · 2023Article
- Nonspecific Binding of Adenosine Tripolyphosphate and Tripolyphosphate Modulates the Phase Behavior of Lysozyme.Journal of the American Chemical Society · 2023Article
- ATP and Tri-Polyphosphate (TPP) Suppress Protein Aggregate Growth by a Supercharging Mechanism.Biomedicines · 2021Article
- Crystallin gene expression: Insights from studies of transcriptional bursting.Experimental eye research · 2021Review
- Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.Structure (London, England : 1993) · 2021Article
- Anomalous Salt Dependence Reveals an Interplay of Attractive and Repulsive Electrostatic Interactions in α-synuclein Fibril Formation.QRB discovery · 2020Article
- Temperature-Dependent Interactions Explain Normal and Inverted Solubility in a γD-Crystallin Mutant.Biophysical journal · 2019Article
- Modeling the depletion effect caused by an addition of polymer to monoclonal antibody solutions.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- Model for screened, charge-regulated electrostatics of an eye lens protein: Bovine gammaB-crystallin.Physical review. E · 2017Article
- Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Nature communications · 2017Article
- Single-shot real-time video recording of a photonic Mach cone induced by a scattered light pulse.Science advances · 2017Article
- Effect of the surface charge distribution on the fluid phase behavior of charged colloids and proteins.The Journal of chemical physics · 2016Article
- Modeling phase transitions in mixtures of β-γ lens crystallins.Soft matter · 2016Article
- Computational crystallization.Archives of biochemistry and biophysics · 2016Review
- The Effect of Attractive Interactions and Macromolecular Crowding on Crystallins Association.PloS one · 2016Article
- Ion-activated attractive patches as a mechanism for controlled protein interactions.Scientific reports · 2014Article
- Role of anisotropic interactions for proteins and patchy nanoparticles.The journal of physical chemistry. B · 2014Article
- Characterizing protein crystal contacts and their role in crystallization: rubredoxin as a case study.Soft matter · 2014Article
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7 authors at 1 institution in 1 country.
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Abstract
The P23T mutant of human gammaD-crystallin (HGD) is associated with cataract. We have previously investigated the solution properties of this mutant, as well as those of the closely related P23V and P23S mutants, and shown that although mutations at site 23 of HGD do not produce a significant structural change in the protein, they nevertheless profoundly alter the solubility of the protein. Remarkably, the solubility of the mutants decreases with increasing temperature, in sharp contrast to the behavior of the native protein. This inverted solubility corresponds to a strong increase in the binding energy with temperature. Here we have investigated the liquid-liquid coexistence curve and the diffusivity of the P23V mutant and find that these solution properties are unaffected by the mutation. This means that the chemical potentials in the solution phase are essentially unaltered. The apparent discrepancy between the interaction energies in the solution phase, as compared with the solid phase, is explicable in terms of highly anisotropic interprotein interactions, which are averaged out in the solution phase but are fully engaged in the solid phase.
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