Abstract
The combination of surface plasmon pesonance (SPR) and mass spectrometry (MS) provides a unique methodology for studying proteins and their interactions. SPR is utilized to assess protein quantitative variations and the kinetic aspects of protein interactions, whereas MS complements the analysis by providing an exclusive look at the structural features of the interacting proteins via measurement of their mass. Thus, intrinsic protein structural modifications that go unregistered via the SPR detection can readily be assessed from the MS data. The purpose of this chapter is dissemination of the procedures and protocols for successful SPR-MS analysis. The individual steps of the complete SPR-MS process are illustrated via analysis of cardiac troponin I (cTnI).
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Nedelkov, D., Nelson, R.W. (2006). Surface Plasmon Resonance Mass Spectrometry for Protein Analysis. In: New and Emerging Proteomic Techniques. Methods in Molecular Biology™, vol 328. Humana Press. https://doi.org/10.1385/1-59745-026-X:131
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DOI: https://doi.org/10.1385/1-59745-026-X:131
Publisher Name: Humana Press
Print ISBN: 978-1-58829-519-4
Online ISBN: 978-1-59745-026-3
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