Abstract
19F NMR has been used as a probe for investigating bioorganic and biological systems for three decades. Recent reviews have touted this nucleus for its unique characteristics that allow probing in vivo biological systems without endogenous signals. 19F nucleus is exceptionally sensitive to molecular and microenvironmental changes and thus can be exploited to explore structure, dynamics, and changes in a protein or molecule in the cellular environment. We show how mass spectrometry can be used to assess and characterize the incorporation of fluorine into proteins. This methodology can be applied to a number of systems where 19F NMR is used.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Danielson MA, Falke JJ (1996) Annu Rev Biophys Biomol Struct 25:163–195
Yu JX, Hallac RR, Chiguru S, Mason RP (2013) Prog Nucl Magn Reson Spectrosc 70:25–49
Reid DG, Murphy PS (2008) Drug Discov Today 13:473–480
Luck LA, Falke JJ (1991) Biochemistry 30:6484–6490
Zemsky J, Rusinova E, Nemerson Y, Luck LA, Ross JB (1999) Proteins 37:709–716
Crabb JW, Carlson A, Chen Y, Goldflam S, Intres R et al (1998) Protein Sci 7:746–757
Crowley PB, Kyne C, Monteith WB (2012) Chem Commun (Camb) 48:10681–10683
Luck LA, Falke JJ (1991) Biochemistry 30:4248–4256
Yu J, Cui D, Zhao D, Mason RP (2008). In: GH A. Tressaud (ed) Fluorine and health. Elsevier B.V., Amsterdam, pp 198–276
Senear DF, Mendelson RA, Stone DB, Luck LA, Rusinova E, Ross JB (2002) Anal Biochem 300:77–86
Buer BC, Marsh EN (2012) Protein Sci 21:453–462
Salwiczek M, Nyakatura EK, Gerling UI, Ye S, Koksch B (2012) Chem Soc Rev 41:2135–2171
Luck LA, Moravan MJ, Garland JE, Salopek-Sondi B, Roy D (2003) Biosens Bioelectron 19:249–259
Carmon KS, Baltus RE, Luck LA (2004) Biochemistry 43:14249–14256
Andreescu S, Luck LA (2008) Anal Biochem 375:282–290
Tripathi A, Wang J, Luck LA, Suni II (2007) Anal Chem 79:1266–1270
Sokolov I, Subba-Rao V, Luck LA (2006) Biophys J 90:1055–1063
Luck LA, Vance JE, O’Connell TM, London RE (1996) J Biomol NMR 7:261–272
Salopek-Sondi B, Luck LA (2002) Protein Eng 15:855–859
Salopek-Sondi B, Skeels MC, Swartz D, Luck LA (2003) Proteins 53:273–281
Salopek-Sondi B, Swartz D, Adams PS, Luck LA (2002) J Biomol Struct Dyn 20:381–387
Ahmed AH, Loh AP, Jane DE, Oswald RE (2007) J Biol Chem 282:12773–12784
Magnusson U, Salopek-Sondi B, Luck LA, Mowbray SL (2004) J Biol Chem 279:8747–8752
Luck LA, Johnson C (2000) Protein Sci 9:2573–2576
Vyas MN, Jacobson BL, Quiocho FA (1989) J Biol Chem 264:20817–20821
Luck LA, Falke JJ (1991) Biochemistry 30:4257–4261
Waxman E, Rusinova E, Hasselbacher CA, Schwartz GP, Laws WR, Ross JB (1993) Anal Biochem 210:425–428
Holzberger B, Obeid S, Welte W, Diederichs K, Marx A (2012) Chem Sci 3:2924–2931
Acknowledgments
The author would like to thank Bruce O’Roarke for analyzing the proteins by mass spectrometry. This work has been supported by the NSF for the LCMS instrumentation in the Chemistry Department at the University of Vermont (CHE MRI-0821501, LAL Co-PI), SUNY at Plattsburgh President’s Award and Mini Grant.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer International Publishing Switzerland
About this chapter
Cite this chapter
Luck, L.A. (2014). Analysis of Fluorinated Proteins by Mass Spectrometry. In: Woods, A., Darie, C. (eds) Advancements of Mass Spectrometry in Biomedical Research. Advances in Experimental Medicine and Biology, vol 806. Springer, Cham. https://doi.org/10.1007/978-3-319-06068-2_14
Download citation
DOI: https://doi.org/10.1007/978-3-319-06068-2_14
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-06067-5
Online ISBN: 978-3-319-06068-2
eBook Packages: Chemistry and Materials ScienceChemistry and Material Science (R0)