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RSS FeedsTemperature-dependent interactions explain normal and inverted solubility in a ?D-crystallin mutant (Biophysical Journal)

 
 

20 july 2019 20:00:51

 
Temperature-dependent interactions explain normal and inverted solubility in a ?D-crystallin mutant (Biophysical Journal)
 


Protein crystal production is a major bottleneck in the structural characterisation of proteins. To advance beyond large-scale screening, rational strategies for protein crystallization are crucial. Understanding how chemical anisotropy (or patchiness) of the protein surface due to the variety of amino acid side chains in contact with solvent, contributes to protein-protein contact formation in the crystal lattice is a major obstacle to predicting and optimising crystallization. The relative scarcity of sophisticated theoretical models that include sufficient detail to link collective behaviour, captured in protein phase diagrams, and molecular level details, determined from high-resolution structural information is a further barrier.


 
182 viewsCategory: Biophysics
 
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