Altered ionization of the B13 Glu in insulin B9 and B10 mutants: a computational analysis

Published date : 23 Aug 2004

An experimentally determined pKa change of +2.50 units has been reported for the B13 Glu residue in a dimeric B9 Ser → Asp insulin mutant relative to the native dimer. Poisson–Boltzmann electrostatics-based pKa calculations were performed to probe the effect of the B9 Ser → Asp and B10 His → Asp mutations on aggregation and the ionization behaviour of the B13 carboxylate.

Journal Paper
Protein Engineering Design and Selection, 2004 Jul;17(7):557-63, doi:10.1093/protein/gzh066
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