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Protein Sample Characterization

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Protein-Ligand Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1008))

Abstract

Most biophysical experiments require protein samples of high quality and accurately determined concentration. This chapter attempts to compile basic information on the most common methods to assess the purity, dispersity, and stability of protein samples. It also reminds of methods to measure protein concentration and of their limits. The idea is to make aware and remind of the range of methods available and of commonly overlooked pitfalls. The aim is to enable experimenters to fully characterize their preparations of soluble or membrane proteins and gain reliable and reproducible results from their experimental work.

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Author information

Authors and Affiliations

  1. ISMB Biophysics Centre, Institute of Structural and Molecular Biology, Birkbeck, University of London, London, UK

    Tina Daviter

  2. Unité G5 Biologie structurale de la sécrétion bactérienne, Institut Pasteur, Paris, France

    Rémi Fronzes

Authors
  1. Tina Daviter
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  2. Rémi Fronzes
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Editor information

Editors and Affiliations

  1. Birbeck, University of London, ISMB Biophysics Centre, Institute of Str, Malet Street, London, WC1E 7HX, United Kingdom

    Mark A. Williams

  2. Birkbeck, University of London, School of Crystallography, ISMB Biophysics Centre, Institute of Str, Malet Street, London, WC1E 7HX, United Kingdom

    Tina Daviter

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Daviter, T., Fronzes, R. (2013). Protein Sample Characterization. In: Williams, M., Daviter, T. (eds) Protein-Ligand Interactions. Methods in Molecular Biology, vol 1008. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-398-5_2

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  • DOI: https://doi.org/10.1007/978-1-62703-398-5_2

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-397-8

  • Online ISBN: 978-1-62703-398-5

  • eBook Packages: Springer Protocols

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