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How to Determine Protein Function by Mass Spectrometry?

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Mass Spectrometry: Developmental Approaches to Answer Biological Questions

Part of the book series: SpringerBriefs in Bioengineering ((BRIEFSBIOENG))

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Abstract

The binding constant and the speed of reaction of proteins and enzymes are pivotal characteristics for some proteins. Such informations are important for example in pharmaceutical research when characterizing the mode of action and the half-life of drugs. Mass spectrometry is a useful tool that could be utilized in the analysis of the binding of compounds of interest to a protein or a receptor. It could also be used to decipher the reaction constants of enzymes. Developmental methods contributed to study and describe the optimal conditions for such analyses. This chapter presents process established to study enzymatic characteristics as well as improvements in terms of mass spectrometry-based study of binding constants.

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References

  1. Deng G, Sanyal G. Applications of mass spectrometry in early stages of target based drug discovery. J Pharm Biomed Anal. 2006;40(3):528–38.

    Article  CAS  Google Scholar 

  2. Tjernberg A, Carnö S, Oliv F, Benkestock K, Edlund PO, Griffiths WJ, Hallén D. Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry. Anal Chem. 2004;76(15):4325–31.

    Article  CAS  Google Scholar 

  3. Loo JA. Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom Rev. 1997;16(1):1–23.

    Article  CAS  Google Scholar 

  4. Sun J, Kitova EN, Klassen JS. Method for stabilizing protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Anal Chem. 2007;79(2):416–25.

    Article  CAS  Google Scholar 

  5. Marcoux J, Robinson CV. Twenty years of gas phase structural biology. Structure. 2013;21(9):1541–50.

    Article  CAS  Google Scholar 

  6. Zhu MM, Rempel DL, Du Z, Gross ML. Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX. J Am Chem Soc. 2003;125(18):5252–3.

    Article  CAS  Google Scholar 

  7. Wortmann A, Jecklin MC, Touboul D, Badertscher M, Zenobi R. Binding constant determination of high-affinity protein-ligand complexes by electrospray ionization mass spectrometry and ligand competition. J Mass Spectrom. 2008;43(5):600–8.

    Article  CAS  Google Scholar 

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Correspondence to Gwenael Pottiez .

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Pottiez, G. (2015). How to Determine Protein Function by Mass Spectrometry?. In: Mass Spectrometry: Developmental Approaches to Answer Biological Questions. SpringerBriefs in Bioengineering. Springer, Cham. https://doi.org/10.1007/978-3-319-13087-3_6

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