Article
Structural hot spots for the solubility of globular proteins.
Nature communications - 24 Feb 2016
Ganesan Ashok, Siekierska Aleksandra, Beerten Jacinte, Brams Marijke, Van Durme Joost, De Baets Greet, Van der Kant Rob, Gallardo Rodrigo, Ramakers Meine, Langenberg Tobias, Wilkinson Hannah, De Smet Frederik, Ulens Chris, Rousseau Frederic, Schymkowitz Joost
Abstract excerpt
Natural selection shapes protein solubility to physiological requirements and recombinant applications that require higher protein concentrations are often problematic. This raises the question whether the solubility of natural protein sequences can be improved. We here show an anti-correlation between the number of aggregation prone regions (APRs) in a protein sequence and its solubility, suggesting that...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.