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• W2759834037 abstract "Abstract Antibodies are central to the growing sector of protein therapeutics, and increasingly they are being manipulated as fragments and combinations. An improved understanding of the properties of antibody domains in isolation would aid in their engineering. We have conducted an analysis of sequence and domain interactions for IgG antibodies and Fab fragments in the structural database. Of sequence-related properties studied, relative lysine to arginine content was found to be higher in CH1 and CL than in variable domains. As earlier work shows that lysine is favoured over arginine in more soluble proteins, this suggests that individual domains may not be optimised for greater solubility, giving scope for fragment engineering. Across other sequence-based features, CH1 is anomalous. A sequence-based scheme predicts CH1 to be folded, although it is known that CH1 folding is linked to IgG assembly and secretion. Calculations indicate that charge interactions in CH1 domains contribute less to folded state stability than in other Fab domains. Expanding to the immunoglobulin superfamily reveals that a subset of non-antibody domains shares sequence composition properties with CH1, leading us to suggest that some of these may also couple folding, assembly and secretion." @default.
• W2759834037 created "2017-10-06" @default.
• W2759834037 creator A5012922833 @default.
• W2759834037 creator A5028066672 @default.
• W2759834037 creator A5075026996 @default.
• W2759834037 date "2017-09-29" @default.
• W2759834037 modified "2023-10-16" @default.
• W2759834037 title "Sequence composition predicts immunoglobulin superfamily members that could share the intrinsically disordered properties of antibody CH1 domains" @default.
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• W2759834037 doi "https://doi.org/10.1038/s41598-017-12616-9" @default.
• W2759834037 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5622106" @default.
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• W2759834037 hasPublicationYear "2017" @default.
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