Abstract
Adding a glycan tag to a protein at a basic residue can be useful in therapeutic applications, because such tags can increase serum half-life, decrease aggregation propensity, or shield immunogenic epitopes of the protein. However, adding such tags to proteins that are not normally glycosylated (naive proteins) can decrease their stability. Culyba et al. (p. [571][1]) added a glycan tag to several naive proteins at an Asn residue in a reverse turn that has a nearby Phe group. The interaction of the aromatic side chains and the glycan allowed energetic stabilization of the proteins. [1]: /lookup/doi/10.1126/science.1198461
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