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asparagine deamidation


Asparagine deamidation could cause charge heterogeneity and hence affect the antibody function if it locates in a binding surface such as CDRs. Deamidated residues are likely susceptible to Aspartate isomerization or result in protein fragmentation, aggregation and immunogenicity. As deamidation is heavily caused by pH and process conditions, careful selection of process parameters to minimize the risks is indispensable. If crystal structure data is available, which allows the most complete assessment of local conformational flexibility and exposure of amino acid residues, combined with primary sequence information, Creative Biolabs guarantee to provide the most accurate prediction of deamidation.

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