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- W4384408240 abstract "ABSTRACT The electrostatic properties of proteins arise from the number and distribution of polar and charged residues. Due to their long-ranged nature, electrostatic interactions in proteins play a critical role in numerous processes, such as molecular recognition, protein solubility, viscosity, and antibody developability. Thus, characterizing and quantifying electrostatic properties of a protein is a pre-requisite for understanding these processes. Here, we present PEP-Patch, a tool to visualize and quantify the electrostatic potential on the protein surface and showcase its applicability to elucidate protease substrate specificity, antibody-antigen recognition and predict heparin column retention times of antibodies as an indicator of pharmacokinetics." @default.
- W4384408240 created "2023-07-16" @default.
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- W4384408240 date "2023-07-15" @default.
- W4384408240 modified "2023-10-18" @default.
- W4384408240 title "PEP-Patch: Electrostatics in Protein-Protein Recognition, Specificity and Antibody Developability" @default.
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- W4384408240 doi "https://doi.org/10.1101/2023.07.14.547811" @default.
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