Abstract
Protein solubility determines the conditions under which the protein will remain in solution. As a result, it is an important quantity in applications that involve concentrated protein solutions. Here I describe the solubility measurement of the protein thaumatin in the presence of tartrate ions as a function of temperature. This method can be used to measure the solubility of other proteins.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
McPherson A (1999) Crystallization of biological macromolecules. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
McManus JJ, Charbonneau P, Zaccarelli E, Asherie N (2016) The physics of protein self-assembly. Curr Opin Colloid Interface Sci 22:73–79
Trevino SR, Scholtz JM, Pace CN (2008) Measuring and increasing protein solubility. J Pharm Sci 97:4155–4166
Benvenuti M, Magnani S (2007) Nat Protoc 2:1633–1651
McPherson A, Gavira JA (2014) Introduction to protein crystallization. Acta Crystallogr F Struct Biol Commun 70(Pt 1):2–20
Astier J-P, Veesler S (2008) Using temperature to crystallize proteins: a mini-review. Cryst Growth Des 8:415–4219
Aldabeideh N, Jones MJ, Myerson AS, Ulrich J (2009) The solubility of orthorhombic lysozyme crystals obtained at high pH. Cryst Growth Des 9:3313–3317
Berland CR, Thurston GM, Kondo M, Broide ML, Pande J, Ogun O, Benedek GB (1992) Solid-liquid phase boundaries of lens protein solutions. Proc Natl Acad Sci U S A 89:1214–1218
Sleutel M, Willaert R, Gillespie C, Evrard C, Wyns L, Maes D (2009) Kinetics and thermodynamics of glucose isomerase crystallization. Cryst Growth Des 9:497–504
Feeling-Taylor AR, Banish RM, Hirsch RE, Vekilov PG (1999) Miniaturized scintillation technique for protein solubility determinations. Rev Sci Instrum 70:2845–2849
Rowe JB, Cancel RA, Evangelous TD, Flynn RP, Pechenov S, Subramony JA, Zhang J, Wang Y (2017) Metastability gap in the phase diagram of monoclonal IgG antibody. Biophys J 113:1750–1756
Ko TP, Day J, Greenwood A, McPherson A (1994) Structures of three crystal forms of the sweet protein thaumatin. Acta Cryst D 50:813–825
Asherie N, Ginsberg C, Blass S, Greenbaum A, Knafo S (2008) Solubility of thaumatin. Cryst Growth Des 8:1815–1817
Asherie N, Ginsberg C, Greenbaum A, Blass S, Knafo S (2008) Effect of protein purity and precipitant stereochemistry on the crystallization of thaumatin. Cryst Growth Des 8:4200–4207
Asherie N (2004) Protein crystallization and phase diagrams. Methods 34:266–272
Acknowledgments
I gratefully acknowledge financial support from the National Science Foundation (DMR 0901260 and 1206416) and Yeshiva University.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Science+Business Media, LLC, part of Springer Nature
About this protocol
Cite this protocol
Asherie, N. (2019). Measuring Protein Solubility. In: McManus, J. (eds) Protein Self-Assembly. Methods in Molecular Biology, vol 2039. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9678-0_4
Download citation
DOI: https://doi.org/10.1007/978-1-4939-9678-0_4
Published:
Publisher Name: Humana, New York, NY
Print ISBN: 978-1-4939-9677-3
Online ISBN: 978-1-4939-9678-0
eBook Packages: Springer Protocols