Evaluating electrostatic contributions to binding with the use of protein charge ladders

Jinming Gao, Mathai Mammen, George M. Whitesides

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Abstract

Electrostatic interactions between charges on ligands and charges on proteins that are remote from the binding interface can influence the free energy of binding (ΔG(b)). The binding affinities between charged ligands and the members of a charge ladder of bovine carbonic anhydrase (CAII) constructed by random acetylation of the amino groups on its surface were measured by affinity capillary electrophoresis (ACE). The values of ΔG(b) derived from this analysis correlated approximately linearly with the charge. Opposite charges on the ligand and the members of the charge ladder of CAII were stabilizing; like charges were destabilizing. The combination of ACE and protein charge ladders provides a tool for quantitatively examining the contributions of electrostatics to free energies of molecular recognition in biology.

Original languageEnglish (US)
Pages (from-to)535-537
Number of pages3
JournalScience
Volume272
Issue number5261
DOIs
StatePublished - Apr 26 1996

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