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PEP-Patch: Electrostatics in Protein–Protein Recognition, Specificity, and Antibody Developability

[Image: see text] The electrostatic properties of proteins arise from the number and distribution of polar and charged residues. Electrostatic interactions in proteins play a critical role in numerous processes such as molecular recognition, protein solubility, viscosity, and antibody developability...

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Detalles Bibliográficos
Autores principales: Hoerschinger, Valentin J., Waibl, Franz, Pomarici, Nancy D., Loeffler, Johannes R., Deane, Charlotte M., Georges, Guy, Kettenberger, Hubert, Fernández-Quintero, Monica L., Liedl, Klaus R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10685443/
https://www.ncbi.nlm.nih.gov/pubmed/37934909
http://dx.doi.org/10.1021/acs.jcim.3c01490
Descripción
Sumario:[Image: see text] The electrostatic properties of proteins arise from the number and distribution of polar and charged residues. 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 are prerequisites for understanding these processes. Here, we present PEP-Patch, a tool to visualize and quantify the electrostatic potential on the protein surface in terms of surface patches, denoting separated areas of the surface with a common physical property. We highlight its applicability to elucidate protease substrate specificity and antibody–antigen recognition and predict heparin column retention times of antibodies as an indicator of pharmacokinetics.