Elsevier

Methods in Enzymology

Volume 130, 1986, Pages 437-453
Methods in Enzymology

[18] Stabilization and destabilization of protein structure by charge interactions

https://doi.org/10.1016/0076-6879(86)30020-XGet rights and content

Publisher Summary

Protein molecules are unique polyelectrolytes and carry their own partial complement of counterions that exhibit charge cancellations at their characteristic isoionic point, and tight binding in the form of intramolecular salt bridges. When the protein's own charge array is sufficiently asymmetric by either composition, geometry, or both, the surface electrostatic potential in the absence of steric hindrance will dictate specific ion binding sites. Any calculation of protein stabilization as a function of pH and ionic strength include the phenomenon of specific ion binding where applicable. Electrostatic stabilization accounts for approximately half of the energy of dimer-tetramer assembly in hemoglobin; its role is marginal in the combination of trypsin with bovine pancreatic trypsin inhibitor (BPTI). Each protein studied shows a specific pattern of stabilization or destabilization resulting from a unique set of long-range, overlapping coulombic fields associated with each charge site. The individual contributions, and hence, the overall stabilization are affected as the array is modified by changes in pH, ionic strength, binding of charge components, or alteration of solvent exposure.

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