cover illustration An albumin binding domain from streptococcal protein G (G148-GA3) was subjected to affinity maturation using a combination of combinatorial protein engineering and rational design. The cover figure shows the three-helix bundle structure of the G148-GA3 domain with the fifteen positions that were variegated for the construction of the library marked in blue and a position at which spontaneous mutations were found marked in green. The variant showing the highest affinity for HSA contained seven amino acid substitutions compared to wild type G148-GA3. These mutations improved the affinity (KD) for HSA by several orders of magnitude, resulting in femtomolar affinity. For further details please see Jonsson et al. pp. 515-527.
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