Molecular thermodynamic properties of protein solutions from partial specific volumes

P. E. Pjura, Michael Paulaitis, A. M. Lenhoff

Research output: Contribution to journalArticle

Abstract

Partial specific volumes at 25°C are reported for α‐chymotrypsinogen in aqueous solutions containing NaCl, citrate, and/or polyethylene gycol (PEG) over a range of protein concentrations. The concentration dependence of the partial specific volume can be either positive or negative, depending on the solvent. For example, the partial specific volume increases with increasing protein concentration in NaCl/citrate solutions at high salt concentrations, and decreases with increasing protein concentration in solutions containing PEG. Kirkwood‐Buff solution theory has been applied to interpret these results, and it was found that the concentration dependence is determined by two factors: (1) the effective or solvent‐averaged interactions between protein molecules in solution, and (2) three‐body protein – protein – solvent and protein – solvent ‐ solvent interactions. An approach is proposed for the experimental determination of both contributions that involves measuring osmotic pressures and volumetric properties of dilute to concentrated protein solutions.

Original languageEnglish (US)
Pages (from-to)1005-1009
Number of pages5
JournalAICHE Journal
Volume41
Issue number4
DOIs
StatePublished - 1995
Externally publishedYes

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Thermodynamics
Density (specific gravity)
Thermodynamic properties
Proteins
Polyethylene
Citric Acid
Polyethylenes
Chymotrypsinogen
Osmotic Pressure
Salts
Molecules

ASJC Scopus subject areas

  • Biotechnology
  • Environmental Engineering
  • Chemical Engineering(all)

Cite this

Molecular thermodynamic properties of protein solutions from partial specific volumes. / Pjura, P. E.; Paulaitis, Michael; Lenhoff, A. M.

In: AICHE Journal, Vol. 41, No. 4, 1995, p. 1005-1009.

Research output: Contribution to journalArticle

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