Fig. 2.
Fig. 2. Predicted secondary folding structure for Ixolaris. / Disulfide bonds are assumed on the basis of the crystal structure of bovine pancreatic trypsin inhibitor.36 The charges of the amino acid side chains are shown. Predicted N-linked glycosylation sites are Asn65, Asn98, and Asn136.

Predicted secondary folding structure for Ixolaris.

Disulfide bonds are assumed on the basis of the crystal structure of bovine pancreatic trypsin inhibitor.36 The charges of the amino acid side chains are shown. Predicted N-linked glycosylation sites are Asn65, Asn98, and Asn136.

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