PEP-Patch: Electrostatics in Protein-Protein Recognition, Specificity and Antibody Developability
F. Waibl, N. D. Pomarici, V. J. Hoerschinger, J. R. Loeffler, C. Deane, G. Georges, H. Kettenberger, M. L. Fernandez-Quintero, K. R. Liedl
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.
02 /Specification & Classification
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