Literature DB >> 19164280

Protein ionizable groups: pK values and their contribution to protein stability and solubility.

C Nick Pace1, Gerald R Grimsley, J Martin Scholtz.   

Abstract

The structure, stability, solubility, and function of proteins depend on their net charge and on the ionization state of the individual residues. Consequently, biochemists are interested in the pK values of the ionizable groups in proteins and how these pK values depend on their environment. We review what has been learned about pK values of ionizable groups in proteins from experimental studies and discuss the important contributions they make to protein stability and solubility.

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Year:  2009        PMID: 19164280      PMCID: PMC2679426          DOI: 10.1074/jbc.R800080200

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  43 in total

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Authors:  G J Lesser; G D Rose
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Authors:  Saul R Trevino; Kuppan Gokulan; Stephanie Newsom; Richard L Thurlkill; Kevin L Shaw; Vladimir A Mitkevich; Alexander A Makarov; James C Sacchettini; J Martin Scholtz; C Nick Pace
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  115 in total

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10.  pKa Calculations with the Polarizable Drude Force Field and Poisson-Boltzmann Solvation Model.

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