Functional assays of membrane-bound proteins with SAMDI-TOF mass spectrometry

Violeta L. Marin*, Timothy H. Bayburt, Stephen G. Sligar, Milan Mrksich

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

51 Scopus citations

Abstract

(Chemical Equation Presented) Delicate probing: When nanodisc assemblies are used to present membrane proteins on a biochip surface, interactions of these proteins can be studied by mass spectrometry. The method is illustrated with the protein rhodopsin, which is immobilized to a self-assembled monolayer by way of a his-tagged membrane scaffold protein. Upon activation of rhodopsin with light, the protein complex transducin binds and can be detected using SAMDI mass spectrometry.

Original languageEnglish (US)
Pages (from-to)8796-8798
Number of pages3
JournalAngewandte Chemie - International Edition
Volume46
Issue number46
DOIs
StatePublished - 2007

Funding

This work was supported by the National Heart, Lung, and Blood Institute (grants HL47887, HL47889, HL47890, HL47892, HL47902, HL55208, and R01 HL58329) and the General Clinic Research Centers Program (grants NCRR GCRC, M01 RR431, and M01 RR01346).

Keywords

  • Biochips
  • Mass spectrometry
  • Monolayers
  • Proteins
  • Rhodopsin

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

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