Surface plasmon resonance mass spectrometry for protein analysis.

Dobrin Nedelkov, Randall W. Nelson

Research output: Contribution to journalArticle

13 Citations (Scopus)

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 SPRMS process are illustrated via analysis of cardiac troponin I (cTnI).

Original languageEnglish (US)
Pages (from-to)131-139
Number of pages9
JournalMethods in molecular biology (Clifton, N.J.)
Volume328
StatePublished - 2006

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Surface Plasmon Resonance
Mass Spectrometry
Proteins
Troponin I

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Surface plasmon resonance mass spectrometry for protein analysis. / Nedelkov, Dobrin; Nelson, Randall W.

In: Methods in molecular biology (Clifton, N.J.), Vol. 328, 2006, p. 131-139.

Research output: Contribution to journalArticle

Nedelkov, Dobrin ; Nelson, Randall W. / Surface plasmon resonance mass spectrometry for protein analysis. In: Methods in molecular biology (Clifton, N.J.). 2006 ; Vol. 328. pp. 131-139.
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